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APR Prediction Models
GAP (Generalized Aggregation Proneness)
ANuPP (Prediciton of Nucleating APRs)
V
L
AmY-Pred (Predicting antibody light chain aggregation)
Aggregation Kinetics Prediction Models
AggreRATE-Disc (Classifying Aggregating Point Mutation)
AggreRATE-Pred (Predicting Aggregation Rate for Point Mutation)
AbsoluRATE (Predicting Absolute aggregation rate)
Amylo-Pipe (Comprehensive aggregation prediction)
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APR Prediction Models:
GAP (Generalized Aggregation Proneness)
ANuPP (Prediciton of Nucleating APRs)
V
L
AmY-Pred (Predicting antibody light chain aggregation)
Aggregation Kinetics Prediction Models:
AggreRATE-Disc (Classifying Aggregating Point Mutation)
AggreRATE-Pred (Predicting Aggregation Rate for Point Mutation)
AbsoluRATE (Predicting Absolute aggregation rate)
Amylo-Pipe (Comprehensive aggregation prediction)
Structure database of aggregation related proteins and peptides
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Displaying 421 to 450 records out of 565 records fetched.
Entry
PDB ID
Protein
Name
Species
Length
Mutation(s)
Class
Type
Method
Resolution (
Å
)
PMID
S-0421
5CKG
Beta-2-microglobulin
Homo sapiens
100
V85E
Amyloid
Protein
X-RAY DIFFRACTION
1.75
27150430
S-0422
5CR1
Transthyretin
Homo sapiens
116
No
Non-amyloid
Inhibitor complex
X-RAY DIFFRACTION
1.54
26468275
S-0423
5DLI
Superoxide dismutase [Cu-Zn]
Homo sapiens
11
No
Non-amyloid
Peptide
X-RAY DIFFRACTION
2.1
28760994
S-0424
5E5V
Islet Amyloid Polypeptide
Homo sapiens
7
No
Amyloid
Fibril
X-RAY DIFFRACTION
1.24
26629790
S-0425
5E5X
Islet Amyloid Polypeptide
Homo sapiens
6
No
Amyloid
Fibril
X-RAY DIFFRACTION
1.61
26629790
S-0426
5E5Z
Islet Amyloid Polypeptide
Homo sapiens
6
No
Amyloid
Fibril
X-RAY DIFFRACTION
1.66
26629790
S-0427
5E61
Islet Amyloid Polypeptide
Homo sapiens
7
No
Amyloid
Fibril
X-RAY DIFFRACTION
1.79
26629790
S-0428
5GIW
Humanin
Homo sapiens
24
D-isomerized serine
Non-amyloid
Inhibitor complex
SOLUTION NMR
27349871
S-0429
5I55
Phenol-soluble modulin alpha 3 peptide
Staphylococcus aureus
22
No
Amyloid
Fibril
X-RAY DIFFRACTION
1.45
28232575
S-0430
5IIW
Superoxide dismutase [Cu-Zn]
Homo sapiens
11
No
Non-amyloid
Peptide
X-RAY DIFFRACTION
2.0
28760994
S-0431
5K1J
Transthyretin
Homo sapiens
116
No
Non-amyloid
Inhibitor complex
X-RAY DIFFRACTION
1.69
27402536
S-0432
5K1N
Transthyretin
Homo sapiens
118
No
Non-amyloid
Inhibitor complex
X-RAY DIFFRACTION
1.81
27402536
S-0433
5K2E
Eukaryotic peptide chain release factor GTP-binding subunit
Saccharomyces cerevisiae
6
No
Amyloid
Fibril
ELECTRON CRYSTALLOGRAPHY
1.0
27647903
S-0434
5K2F
Eukaryotic peptide chain release factor GTP-binding subunit
Saccharomyces cerevisiae
6
No
Amyloid
Fibril
ELECTRON CRYSTALLOGRAPHY
1.0
27647903
S-0435
5K2G
Eukaryotic peptide chain release factor GTP-binding subunit
Saccharomyces cerevisiae
7
No
Amyloid
Fibril
ELECTRON CRYSTALLOGRAPHY
1.1
27647903
S-0436
5K2H
Eukaryotic peptide chain release factor GTP-binding subunit
Saccharomyces cerevisiae
7
No
Amyloid
Fibril
ELECTRON CRYSTALLOGRAPHY
1.05
27647903
S-0437
5K7N
Microtubule-associated protein tau
Homo sapiens
6
No
Amyloid
Fibril
ELECTRON CRYSTALLOGRAPHY
1.1
28192420
S-0438
5KK3
Amyloid-beta A4 protein
Homo sapiens
42
No
Amyloid
Fibril
SOLID-STATE NMR
27355699
S-0439
5KNZ
Islet amyloid polypeptide
Homo sapiens
11
S20G
Amyloid
Fibril
ELECTRON CRYSTALLOGRAPHY
1.9
S-0440
5KO0
Islet amyloid polypeptide
Homo sapiens
11
No
Amyloid
Fibril
ELECTRON CRYSTALLOGRAPHY
1.4
S-0441
5L6Q
AL protein
Homo sapiens
115
No
Amyloid
Protein
X-RAY DIFFRACTION
1.4
28544119
S-0442
5L6R
Major prion protein
Homo sapiens
145
No
Amyloid
Protein
SOLUTION NMR
28109886
S-0443
5LFY
Amyloid-beta A4 protein
Homo sapiens
11
D7H
Amyloid
Peptide
SOLUTION NMR
28570778
S-0444
5M6A
Bence-Jones light chain dimer H9
Homo sapiens
216
No
Amyloid
Protein
X-RAY DIFFRACTION
1.64
29196671
S-0445
5M6I
Bence-Jones light chain dimer M8
216
No
Non-amyloid
Protein
X-RAY DIFFRACTION
2.2
29196671
S-0446
5M76
Bence-Jones light chain dimer H10
Homo sapiens
215
No
Amyloid
Protein
X-RAY DIFFRACTION
2.5
29196671
S-0447
5MGQ
Islet amyloid polypeptide
Homo sapiens
37
No
Amyloid
Peptide
SOLUTION NMR
28287098
S-0448
5MTL
IGL@ protein
Homo sapiens
216
No
Amyloid
Protein
X-RAY DIFFRACTION
2.45
29196671
S-0449
5MUD
Immunoglobin light chain dimer H6
Homo sapiens
216
No
Amyloid
Protein
X-RAY DIFFRACTION
2.34
29196671
S-0450
5MUH
Immunoglobin light chain dimer H7
Homo sapiens
212
No
Amyloid
Protein
X-RAY DIFFRACTION
2.65
29196671
Entry:S-0421
PDB ID: 5CKG
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Protein Contacts Atlas
Sequence & Sec. Str.
Chain 1
1
M
I
Q
R
T
P
K
I
Q
V
Y
S
R
H
P
A
E
N
G
K
S
N
F
L
N
25
26
C
Y
V
S
G
F
H
P
S
D
I
E
V
D
L
L
K
N
G
E
R
I
E
K
V
50
51
E
H
S
D
L
S
F
S
K
D
W
S
F
Y
L
L
Y
Y
T
E
F
T
P
T
E
75
76
K
D
E
Y
A
C
R
V
N
H
E
T
L
S
Q
P
K
I
V
K
W
D
R
D
M
100
Chain 2
1
M
I
Q
R
T
P
K
I
Q
V
Y
S
R
H
P
A
E
N
G
K
S
N
F
L
N
25
26
C
Y
V
S
G
F
H
P
S
D
I
E
V
D
L
L
K
N
G
E
R
I
E
K
V
50
51
E
H
S
D
L
S
F
S
K
D
W
S
F
Y
L
L
Y
Y
T
E
F
T
P
T
E
75
76
K
D
E
Y
A
C
R
V
N
H
E
T
L
S
Q
P
K
I
V
K
W
D
R
D
M
100
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Human beta-2 microglobulin mutant V85E
They compare the native state dynamics of Beta-2 microglobulin (Beta2m), whose aggregation is associated with dialysis-related amyloidosis, and its aggregation-resistant mutant W60G. Their results indicate that W60G low aggregation propensity can be explained, beyond its higher stability, by an increased average protection of the aggregation-prone residues at its surface. To validate these findings, They designed Beta2m variants that alter the aggregation-prone exposed surface of wild-type and W60G Beta2m modifying their aggregation propensity.
Literature
PMID:
27150430
Author(s):
Camilloni, C., Sala, B.M., Sormanni, P., Porcari, R., Corazza, A., De Rosa, M., Zanini, S., Barbiroli, A., Esposito, G., Bolognesi, M., Bellotti, V., Vendruscolo, M., Ricagno, S.
Reference:
Sci Rep. 2016 May 6;6:25559.
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Entry:
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Structure:
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Contact Network:
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Protein Information
Protein Name:
Beta-2-microglobulin
Alternative Name:
Gene Name:
B2M, CDABP0092, HDCMA22P
Sequence Length:
100
Species:
Homo sapiens
Mutation(s):
V85E
E.C. Number:
UniProt ID:
P61769
Keyword(s):
Beta-2-microglobulin
Structure Information
PDB ID:
5CKG
Amyloid Category:
Amyloid
Type:
Protein
Global Stoichiometry:
Monomer - A
PDB Classification:
IMMUNE SYSTEM
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
1.75
R free:
0.23199999
Ligand Information
Ligand ID
Chain ID
Ligand Formula
Ligand MW
Ligand Name
Ligand SMILES
InChI Key
ACT
A
C2 H3 O2 -1
59.04
ACETATE ION
CC(=O)[O-]
QTBSBXVTEAMEQO-UHFFFAOYSA-M
ACT
B
C2 H3 O2 -1
59.04
ACETATE ION
CC(=O)[O-]
QTBSBXVTEAMEQO-UHFFFAOYSA-M
GOL
B
C3 H8 O3
92.09
GLYCEROL
C(C(CO)O)O
PEDCQBHIVMGVHV-UHFFFAOYSA-N
Entry:S-0422
PDB ID: 5CR1
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Protein Contacts Atlas
Sequence & Sec. Str.
Chain 1
1
C
P
L
M
V
K
V
L
D
A
V
R
G
S
P
A
I
N
V
A
V
H
V
F
R
25
26
K
A
A
D
D
T
W
E
P
F
A
S
G
K
T
S
E
S
G
E
L
H
G
L
T
50
51
T
E
E
E
F
V
E
G
I
Y
K
V
E
I
D
T
K
S
Y
W
K
A
L
G
S
75
76
S
P
F
H
E
H
A
E
V
V
F
T
A
N
D
S
G
P
R
R
Y
T
I
A
A
100
101
L
L
S
P
Y
S
Y
S
T
T
A
V
V
T
N
P
116
Chain 2
1
C
P
L
M
V
K
V
L
D
A
V
R
G
S
P
A
I
N
V
A
V
H
V
F
R
25
26
K
A
A
D
D
T
W
E
P
F
A
S
G
K
T
S
E
S
G
E
L
H
G
L
T
50
51
T
E
E
E
F
V
E
G
I
Y
K
V
E
I
D
T
K
S
Y
W
K
A
L
G
S
75
76
S
P
F
H
E
H
A
E
V
V
F
T
A
N
D
S
G
P
R
R
Y
T
I
A
A
100
101
L
L
S
P
Y
S
Y
S
T
T
A
V
V
T
N
P
116
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Crystal structure of TTR/resveratrol/T4 complex
A main finding of this investigation was the highly preferential binding of resveratrol and thyroxine, both characterized by negative binding cooperativity, to distinct sites in TTR, consistent with the data of x-ray analysis of TTR in complex with both ligands. Although revealing the ability of the two thyroxine binding sites of TTR to discriminate between different ligands, this feature has allowed us to evaluate the interactions of polyphenols with both resveratrol and thyroxine preferential binding sites. Among flavonoids, genistein and apigenin were able to effectively displace resveratrol from its preferential binding site, whereas genistein also showed the ability to interact, albeit weakly, with the preferential thyroxine binding site. Several glucuronidated polyphenol metabolites did not exhibit significant competition for resveratrol and thyroxine preferential binding sites and lacked the ability to stabilize TTR. However, resveratrol-3-O-sulfate was able to significantly protect the protein native state.
Literature
PMID:
26468275
Author(s):
Florio, P., Folli, C., Cianci, M., Del Rio, D., Zanotti, G., Berni, R.
Reference:
J Biol Chem. 2015 Dec 11;290(50):29769-80.
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Entry:
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Structure:
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Contact Network:
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Protein Information
Protein Name:
Transthyretin
Alternative Name:
ATTR, Prealbumin, TBPA
Gene Name:
TTR, PALB
Sequence Length:
116
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
P02766
Keyword(s):
Transthyretin
Structure Information
PDB ID:
5CR1
Amyloid Category:
Non-amyloid
Type:
Inhibitor complex
Global Stoichiometry:
Homo 4-mer - A4
PDB Classification:
TRANSPORT PROTEIN
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
1.54
R free:
0.193
Ligand Information
Ligand ID
Chain ID
Ligand Formula
Ligand MW
Ligand Name
Ligand SMILES
InChI Key
T44
A
C15 H11 I4 N O4
776.87
3,5,3',5'-TETRAIODO-L-THYRONINE
c1c(cc(c(c1I)Oc2cc(c(c(c2)I)O)I)I)C[C@@H](C(=O)O)N
XUIIKFGFIJCVMT-LBPRGKRZSA-N
STL
B
C14 H12 O3
228.24
RESVERATROL
c1cc(ccc1C=Cc2cc(cc(c2)O)O)O
LUKBXSAWLPMMSZ-OWOJBTEDSA-N
Entry:S-0423
PDB ID: 5DLI
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Sequence & Sec. Str.
Chain 1
1
K
V
K
V
W
G
S
I
K
G
L
11
Chain 2
1
K
V
K
V
W
G
S
I
K
G
L
11
Chain 3
1
K
V
K
V
W
G
S
I
K
G
L
11
Chain 4
1
K
V
K
V
W
G
S
I
K
G
L
11
Chain 5
1
K
V
K
V
W
G
S
I
K
G
L
11
Chain 6
1
K
V
K
V
W
G
S
I
K
G
L
11
Chain 7
1
K
V
K
V
W
G
S
I
K
G
L
11
Chain 8
1
K
V
K
V
W
G
S
I
K
G
L
11
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Corkscrew assembly of SOD1 residues 28-38
They determine the corkscrew-like structure of a cytotoxic segment of superoxide dismutase 1 (SOD1) in its oligomeric state. Residues 28–38 of SOD1 (with the sequence PVKVWGSIKGL) have the potential to form a toxic amyloid oligomers. To increase solubility for crystallization, they engineered a single-residue substitution: P28K. The crystal structure shows a twisted Beta-sheet built of antiparallel, out-of-register Beta-strands. Describing its shape, they term it the “corkscrewâ€.
Literature
PMID:
28760994
Author(s):
Sangwan, S., Zhao, A., Adams, K.L., Jayson, C.K., Sawaya, M.R., Guenther, E.L., Pan, A.C., Ngo, J., Moore, D.M., Soriaga, A.B., Do, T.D., Goldschmidt, L., Nelson, R., Bowers, M.T., Koehler, C.M., Shaw, D.E., Novitch, B.G., Eisenberg, D.S.
Reference:
Proc Natl Acad Sci U S A. 2017 Aug 15;114(33):8770-8775.
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Entry:
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Protein Information
Protein Name:
Superoxide dismutase [Cu-Zn]
Alternative Name:
Gene Name:
Sequence Length:
11
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
1.15.1.1
UniProt ID:
P00441
Keyword(s):
Superoxide dismutase [Cu-Zn]
Structure Information
PDB ID:
5DLI
Amyloid Category:
Non-amyloid
Type:
Peptide
Global Stoichiometry:
Homo 8-mer - A8
PDB Classification:
UNKNOWN FUNCTION
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
2.1
R free:
0.262
Ligand Information
Ligand ID
Chain ID
Ligand Formula
Ligand MW
Ligand Name
Ligand SMILES
InChI Key
GOL
B
C3 H8 O3
92.09
GLYCEROL
C(C(CO)O)O
PEDCQBHIVMGVHV-UHFFFAOYSA-N
IOD
D
I -1
126.9
IODIDE ION
[I-]
XMBWDFGMSWQBCA-UHFFFAOYSA-M
Entry:S-0424
PDB ID: 5E5V
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Sequence & Sec. Str.
Chain 1
1
N
F
G
A
I
L
S
7
Chain 2
1
N
F
G
A
I
L
S
7
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Structure of amyloid forming peptide NFGAILS (residues 22-28) from Islet Amyloid Polypeptide
They determined four new crystal structures of segments within IAPP, all forming steric zippers. One of the segments in the fibril core of IAPP forms an out-of-register steric zipper. Analysis of this structure reveals several commonalities with previously solved out-of-register fibrils. These results provide additional evidence of out-of-register Beta sheets as a common structural motif in amyloid aggregates.
Literature
PMID:
26629790
Author(s):
Soriaga, A.B., Sangwan, S., Macdonald, R., Sawaya, M.R., Eisenberg, D.
Reference:
J Phys Chem B. 2016 Jul 7;120(26):5810-6.
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Entry:
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Protein Information
Protein Name:
Islet Amyloid Polypeptide
Alternative Name:
Gene Name:
Sequence Length:
7
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
Keyword(s):
NFGAILS (22-28) from islet amyloid polypeptide, synthesized
Structure Information
PDB ID:
5E5V
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
Homo 12-mer - A12
PDB Classification:
de novo protein
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
1.24
R free:
0.20600000
Entry:S-0425
PDB ID: 5E5X
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Sequence & Sec. Str.
Chain 1
1
A
N
F
L
V
H
6
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Structure of the amyloid forming peptide ANFLVH (residues 13-18) from islet amyloid polypeptide
They determined four new crystal structures of segments within IAPP, all forming steric zippers. One of the segments in the fibril core of IAPP forms an out-of-register steric zipper. Analysis of this structure reveals several commonalities with previously solved out-of-register fibrils. These results provide additional evidence of out-of-register Beta sheets as a common structural motif in amyloid aggregates.
Literature
PMID:
26629790
Author(s):
Soriaga, A.B., Sangwan, S., Macdonald, R., Sawaya, M.R., Eisenberg, D.
Reference:
J Phys Chem B. 2016 Jul 7;120(26):5810-6.
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Entry:
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Structure:
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Protein Information
Protein Name:
Islet Amyloid Polypeptide
Alternative Name:
Gene Name:
Sequence Length:
6
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
Keyword(s):
ANFLVH (residues 13-18) from islet amyloid polypeptide
Structure Information
PDB ID:
5E5X
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
Homo 10-mer - A10
PDB Classification:
de novo protein
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
1.61
R free:
0.161
Entry:S-0426
PDB ID: 5E5Z
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Sequence & Sec. Str.
Chain 1
1
L
V
H
S
S
N
6
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Structure of the amyloid forming peptide LVHSSN
They determined four new crystal structures of segments within IAPP, all forming steric zippers. One of the segments in the fibril core of IAPP forms an out-of-register steric zipper. Analysis of this structure reveals several commonalities with previously solved out-of-register fibrils. These results provide additional evidence of out-of-register Beta sheets as a common structural motif in amyloid aggregates.
Literature
PMID:
26629790
Author(s):
Soriaga, A.B., Sangwan, S., Macdonald, R., Sawaya, M.R., Eisenberg, D.
Reference:
J Phys Chem B. 2016 Jul 7;120(26):5810-6.
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Entry:
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Structure:
PDB
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FASTA
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Protein Information
Protein Name:
Islet Amyloid Polypeptide
Alternative Name:
Gene Name:
Sequence Length:
6
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
Keyword(s):
LVHSSN (residues 16-21) from islet amyloid polypeptide
Structure Information
PDB ID:
5E5Z
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
Homo 10-mer - A10
PDB Classification:
de novo protein
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
1.66
R free:
0.198
Entry:S-0427
PDB ID: 5E61
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Sequence & Sec. Str.
Chain 1
1
F
G
A
I
L
S
S
7
Chain 2
1
F
G
A
I
L
S
S
7
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Structure of amyloid-forming peptide FGAILSS (residues 23-29) from islet amyloid polypeptide
They determined four new crystal structures of segments within IAPP, all forming steric zippers. One of the segments in the fibril core of IAPP forms an out-of-register steric zipper. Analysis of this structure reveals several commonalities with previously solved out-of-register fibrils. These results provide additional evidence of out-of-register Beta sheets as a common structural motif in amyloid aggregates.
Literature
PMID:
26629790
Author(s):
Soriaga, A.B., Sangwan, S., Macdonald, R., Sawaya, M.R., Eisenberg, D.
Reference:
J Phys Chem B. 2016 Jul 7;120(26):5810-6.
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Protein Information
Protein Name:
Islet Amyloid Polypeptide
Alternative Name:
Gene Name:
Sequence Length:
7
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
Keyword(s):
FGAILSS (residues 23-29) from islet amyloid polypeptide
Structure Information
PDB ID:
5E61
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
Homo 11-mer - A11
PDB Classification:
de novo protein
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
1.79
R free:
0.218
Entry:S-0428
PDB ID: 5GIW
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Sequence & Sec. Str.
Chain 1
1
M
A
P
R
G
F
S
C
L
L
L
L
T
S
E
I
D
L
P
V
K
R
R
A
24
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Solution NMR structure of Humanin containing a D-isomerized serine residue
They demonstrated that Humanin d-Ser14 exhibited potent inhibitory activity against fibrillation of amyloid-Beta and remarkably higher binding affinity for amyloid-Beta than that of the Humanin wild-type and S14G mutant. The solution structure of Humanin d-Ser14 showed that d-isomerization of the Ser14 residue enables drastic conformational rearrangement of Humanin. Furthermore, they identified an amyloid-Beta-binding site on Humanin d-Ser14.
Literature
PMID:
27349871
Author(s):
Alsanousi, N., Sugiki, T., Furuita, K., So, M., Lee, Y.H., Fujiwara, T., Kojima, C.
Reference:
Biochem Biophys Res Commun. 2016 Sep 2;477(4):647-653.
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Protein Information
Protein Name:
Humanin
Alternative Name:
Humanin mitochondrial
Gene Name:
MT-RNR2, HN
Sequence Length:
24
Species:
Homo sapiens
Mutation(s):
D-isomerized serine
E.C. Number:
UniProt ID:
Q8IVG9
Keyword(s):
Humanin
Structure Information
PDB ID:
5GIW
Amyloid Category:
Non-amyloid
Type:
Inhibitor complex
Global Stoichiometry:
Monomer - A
PDB Classification:
APOPTOSIS
Method:
SOLUTION NMR
Resolution (
Å
):
R free:
Ligand Information
Ligand ID
Chain ID
Ligand Formula
Ligand MW
Ligand Name
Ligand SMILES
InChI Key
DSN
X
C3 H7 N O3
105.09
D-SERINE
C([C@H](C(=O)O)N)O
MTCFGRXMJLQNBG-UWTATZPHSA-N
Entry:S-0429
PDB ID: 5I55
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Sequence & Sec. Str.
Chain 1
1
M
E
F
V
A
K
L
F
K
F
F
K
D
L
L
G
K
F
L
G
N
N
22
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Crystal Structure of the Virulent PSM-alpha3 Peptide Forming a Cross-alpha amyloid-like Fibril
"The crystal structure of full-length PSMAlpha3 revealed a distinctive ""cross-Alpha"" amyloid-like architecture, in which amphipathic Alpha helices stacked perpendicular to the fibril axis into tight self-associating sheets. "
Literature
PMID:
28232575
Author(s):
Tayeb-Fligelman, E., Tabachnikov, O., Moshe, A., Goldshmidt-Tran, O., Sawaya, M.R., Coquelle, N., Colletier, J.P., Landau, M.
Reference:
Science. 2017 Feb 24;355(6327):831-833.
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Protein Information
Protein Name:
Phenol-soluble modulin alpha 3 peptide
Alternative Name:
Gene Name:
psmA3, SAOUHSC_00411.2
Sequence Length:
22
Species:
Staphylococcus aureus
Mutation(s):
No
E.C. Number:
UniProt ID:
P0C805
Keyword(s):
Psm alpha-3
Structure Information
PDB ID:
5I55
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
Homo 20-mer - A20
PDB Classification:
PROTEIN FIBRIL
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
1.45
R free:
0.184
Ligand Information
Ligand ID
Chain ID
Ligand Formula
Ligand MW
Ligand Name
Ligand SMILES
InChI Key
ACT
A
C2 H3 O2 -1
59.04
ACETATE ION
CC(=O)[O-]
QTBSBXVTEAMEQO-UHFFFAOYSA-M
MPD
A
C6 H14 O2
118.17
(4S)-2-METHYL-2,4-PENTANEDIOL
C[C@@H](CC(C)(C)O)O
SVTBMSDMJJWYQN-YFKPBYRVSA-N
MSE
A
C5 H11 N O2 Se
196.11
SELENOMETHIONINE
C[Se]CC[C@@H](C(=O)O)N
RJFAYQIBOAGBLC-BYPYZUCNSA-N
Entry:S-0430
PDB ID: 5IIW
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Protein Contacts Atlas
Sequence & Sec. Str.
Chain 1
1
K
V
K
V
W
G
S
I
K
G
L
11
Chain 2
1
K
V
K
V
W
G
S
I
K
G
L
11
Chain 3
1
K
V
K
V
W
G
S
I
K
G
L
11
Chain 4
1
K
V
K
V
W
G
S
I
K
G
L
11
Chain 5
1
K
V
K
V
W
G
S
I
K
G
L
11
Chain 6
1
K
V
K
V
W
G
S
I
K
G
L
11
Chain 7
1
K
V
K
V
W
G
S
I
K
G
L
11
Chain 8
1
K
V
K
V
W
G
S
I
K
G
L
11
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Corkscrew assembly of SOD1 residues 28-38 without potassium iodide
They determine the corkscrew-like structure of a cytotoxic segment of superoxide dismutase 1 (SOD1) in its oligomeric state. Residues 28–38 of SOD1 (with the sequence PVKVWGSIKGL) have the potential to form a toxic amyloid oligomers. To increase solubility for crystallization, they engineered a single-residue substitution: P28K. The crystal structure shows a twisted Beta-sheet built of antiparallel, out-of-register Beta-strands. Describing its shape, they term it the “corkscrewâ€.
Literature
PMID:
28760994
Author(s):
Sangwan, S., Zhao, A., Adams, K.L., Jayson, C.K., Sawaya, M.R., Guenther, E.L., Pan, A.C., Ngo, J., Moore, D.M., Soriaga, A.B., Do, T.D., Goldschmidt, L., Nelson, R., Bowers, M.T., Koehler, C.M., Shaw, D.E., Novitch, B.G., Eisenberg, D.S.
Reference:
Proc Natl Acad Sci U S A. 2017 Aug 15;114(33):8770-8775.
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Protein Information
Protein Name:
Superoxide dismutase [Cu-Zn]
Alternative Name:
Gene Name:
Sequence Length:
11
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
1.15.1.1
UniProt ID:
P00441
Keyword(s):
Superoxide dismutase [Cu-Zn]
Structure Information
PDB ID:
5IIW
Amyloid Category:
Non-amyloid
Type:
Peptide
Global Stoichiometry:
Homo 8-mer - A8
PDB Classification:
UNKNOWN FUNCTION
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
2.0
R free:
0.252
Entry:S-0431
PDB ID: 5K1J
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Protein Contacts Atlas
Sequence & Sec. Str.
Chain 1
1
C
P
L
M
V
K
V
L
D
A
V
R
G
S
P
A
I
N
V
A
V
H
V
F
R
25
26
K
A
A
D
D
T
W
E
P
F
A
S
G
K
T
S
E
S
G
E
L
H
G
L
T
50
51
T
E
E
E
F
V
E
G
I
Y
K
V
E
I
D
T
K
S
Y
W
K
A
L
G
I
75
76
S
P
F
H
E
H
A
E
V
V
F
T
A
N
D
S
G
P
R
R
Y
T
I
A
A
100
101
L
L
S
P
Y
S
Y
S
T
T
A
V
V
T
N
P
116
Chain 2
1
C
P
L
M
V
K
V
L
D
A
V
R
G
S
P
A
I
N
V
A
V
H
V
F
R
25
26
K
A
A
D
D
T
W
E
P
F
A
S
G
K
T
S
E
S
G
E
L
H
G
L
T
50
51
T
E
E
E
F
V
E
G
I
Y
K
V
E
I
D
T
K
S
Y
W
K
A
L
G
I
75
76
S
P
F
H
E
H
A
E
V
V
F
T
A
N
D
S
G
P
R
R
Y
T
I
A
A
100
101
L
L
S
P
Y
S
Y
S
T
T
A
V
V
T
N
P
116
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Human TTR altered by a rhenium tris-carbonyl Pyta-C8 derivative
Soaking TTR crystals in a solution containing rhenium tris-carbonyl derivatives yields a TTR conformer never observed before. Only one of the two monomers of the crystallographic dimer is significantly altered, and the inner part of the T4 binding cavity is expanded at one end and shrunk at the other. The result redefines the mechanism of allosteric communication between the two sites, suggesting that negative cooperativity is a function of dimer asymmetry, which can be induced through internal or external binding.
Literature
PMID:
27402536
Author(s):
Ciccone, L., Policar, C., Stura, E.A., Shepard, W.
Reference:
J Struct Biol. 2016 Sep;195(3):353-364.
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Protein Information
Protein Name:
Transthyretin
Alternative Name:
ATTR, Prealbumin, TBPA
Gene Name:
TTR, PALB
Sequence Length:
116
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
P02766
Keyword(s):
Transthyretin
Structure Information
PDB ID:
5K1J
Amyloid Category:
Non-amyloid
Type:
Inhibitor complex
Global Stoichiometry:
Homo 4-mer - A4
PDB Classification:
TRANSPORT PROTEIN
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
1.69
R free:
0.222
Ligand Information
Ligand ID
Chain ID
Ligand Formula
Ligand MW
Ligand Name
Ligand SMILES
InChI Key
ACT
A
C2 H3 O2 -1
59.04
ACETATE ION
CC(=O)[O-]
QTBSBXVTEAMEQO-UHFFFAOYSA-M
DMS
A
C2 H6 O S
78.13
DIMETHYL SULFOXIDE
CS(=O)C
IAZDPXIOMUYVGZ-UHFFFAOYSA-N
EDO
A
C2 H6 O2
62.07
1,2-ETHANEDIOL
C(CO)O
LYCAIKOWRPUZTN-UHFFFAOYSA-N
RE
A
Re
186.21
RHENIUM
[Re]
WUAPFZMCVAUBPE-UHFFFAOYSA-N
DMS
B
C2 H6 O S
78.13
DIMETHYL SULFOXIDE
CS(=O)C
IAZDPXIOMUYVGZ-UHFFFAOYSA-N
EDO
B
C2 H6 O2
62.07
1,2-ETHANEDIOL
C(CO)O
LYCAIKOWRPUZTN-UHFFFAOYSA-N
IMD
B
C3 H5 N2 1
69.08
IMIDAZOLE
c1c[nH+]c[nH]1
RAXXELZNTBOGNW-UHFFFAOYSA-O
RE
B
Re
186.21
RHENIUM
[Re]
WUAPFZMCVAUBPE-UHFFFAOYSA-N
Entry:S-0432
PDB ID: 5K1N
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Protein Contacts Atlas
Sequence & Sec. Str.
Chain 1
1
C
P
L
M
V
K
V
L
D
A
V
R
G
S
P
A
I
N
V
A
V
H
V
F
R
25
26
K
A
A
D
D
T
W
E
P
F
A
S
G
K
T
S
E
S
G
E
L
H
G
L
T
50
51
T
E
E
E
F
V
E
G
I
Y
K
V
E
I
D
T
K
S
Y
W
K
A
L
G
I
75
76
S
P
F
H
E
H
A
E
V
V
F
T
A
N
D
S
G
P
R
R
Y
T
I
A
A
100
101
L
L
S
P
Y
S
Y
S
T
T
A
V
V
T
N
P
K
E
118
Chain 2
1
C
P
L
M
V
K
V
L
D
A
V
R
G
S
P
A
I
N
V
A
V
H
V
F
R
25
26
K
A
A
D
D
T
W
E
P
F
A
S
G
K
T
S
E
S
G
E
L
H
G
L
T
50
51
T
E
E
E
F
V
E
G
I
Y
K
V
E
I
D
T
K
S
Y
W
K
A
L
G
I
75
76
S
P
F
H
E
H
A
E
V
V
F
T
A
N
D
S
G
P
R
R
Y
T
I
A
A
100
101
L
L
S
P
Y
S
Y
S
T
T
A
V
V
T
N
P
K
E
118
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Human TTR altered by a rhenium tris-carbonyl Pyta-C12 derivative
Soaking TTR crystals in a solution containing rhenium tris-carbonyl derivatives yields a TTR conformer never observed before. Only one of the two monomers of the crystallographic dimer is significantly altered, and the inner part of the T4 binding cavity is expanded at one end and shrunk at the other. The result redefines the mechanism of allosteric communication between the two sites, suggesting that negative cooperativity is a function of dimer asymmetry, which can be induced through internal or external binding.
Literature
PMID:
27402536
Author(s):
Ciccone, L., Policar, C., Stura, E.A., Shepard, W.
Reference:
J Struct Biol. 2016 Sep;195(3):353-364.
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Entry:
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Structure:
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Protein Information
Protein Name:
Transthyretin
Alternative Name:
ATTR, Prealbumin, TBPA
Gene Name:
TTR, PALB
Sequence Length:
118
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
P02766
Keyword(s):
Transthyretin
Structure Information
PDB ID:
5K1N
Amyloid Category:
Non-amyloid
Type:
Inhibitor complex
Global Stoichiometry:
Homo 4-mer - A4
PDB Classification:
TRANSPORT PROTEIN
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
1.81
R free:
0.22399999
Ligand Information
Ligand ID
Chain ID
Ligand Formula
Ligand MW
Ligand Name
Ligand SMILES
InChI Key
ACT
A
C2 H3 O2 -1
59.04
ACETATE ION
CC(=O)[O-]
QTBSBXVTEAMEQO-UHFFFAOYSA-M
EDO
A
C2 H6 O2
62.07
1,2-ETHANEDIOL
C(CO)O
LYCAIKOWRPUZTN-UHFFFAOYSA-N
PEG
A
C4 H10 O3
106.12
DI(HYDROXYETHYL)ETHER
C(COCCO)O
MTHSVFCYNBDYFN-UHFFFAOYSA-N
RE
A
Re
186.21
RHENIUM
[Re]
WUAPFZMCVAUBPE-UHFFFAOYSA-N
DMS
B
C2 H6 O S
78.13
DIMETHYL SULFOXIDE
CS(=O)C
IAZDPXIOMUYVGZ-UHFFFAOYSA-N
IMD
B
C3 H5 N2 1
69.08
IMIDAZOLE
c1c[nH+]c[nH]1
RAXXELZNTBOGNW-UHFFFAOYSA-O
RE
B
Re
186.21
RHENIUM
[Re]
WUAPFZMCVAUBPE-UHFFFAOYSA-N
Entry:S-0433
PDB ID: 5K2E
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Sequence & Sec. Str.
Chain 1
1
N
N
Q
Q
N
Y
6
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Structure of NNQQNY from yeast prion Sup35 with zinc acetate determined by MicroED
They show with four structures of the amyloid core of the Sup35 prion protein that, if the diffraction resolution is high enough, sufficiently accurate phases can be obtained by direct methods with the cryo-EM method microelectron diffraction (MicroED), just as in X-ray diffraction.
Literature
PMID:
27647903
Author(s):
Sawaya, M.R., Rodriguez, J., Cascio, D., Collazo, M.J., Shi, D., Reyes, F.E., Hattne, J., Gonen, T., Eisenberg, D.S.
Reference:
Proc Natl Acad Sci U S A. 2016 Oct 4;113(40):11232-11236. Epub 2016 Sep 19
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Protein Information
Protein Name:
Eukaryotic peptide chain release factor GTP-binding subunit
Alternative Name:
Gene Name:
Sequence Length:
6
Species:
Saccharomyces cerevisiae
Mutation(s):
No
E.C. Number:
UniProt ID:
P05453
Keyword(s):
Eukaryotic peptide chain release factor GTP-binding subunit
Structure Information
PDB ID:
5K2E
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
Homo 18-mer - A18
PDB Classification:
PROTEIN FIBRIL
Method:
ELECTRON CRYSTALLOGRAPHY
Resolution (
Å
):
1.0
R free:
0.19399999
Ligand Information
Ligand ID
Chain ID
Ligand Formula
Ligand MW
Ligand Name
Ligand SMILES
InChI Key
ACY
A
C2 H4 O2
60.05
ACETIC ACID
CC(=O)O
QTBSBXVTEAMEQO-UHFFFAOYSA-N
ZN
A
Zn 2
65.41
ZINC ION
[Zn+2]
PTFCDOFLOPIGGS-UHFFFAOYSA-N
Entry:S-0434
PDB ID: 5K2F
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Sequence & Sec. Str.
Chain 1
1
N
N
Q
Q
N
Y
6
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Structure of NNQQNY from yeast prion Sup35 with cadmium acetate determined by MicroED
They show with four structures of the amyloid core of the Sup35 prion protein that, if the diffraction resolution is high enough, sufficiently accurate phases can be obtained by direct methods with the cryo-EM method microelectron diffraction (MicroED), just as in X-ray diffraction.
Literature
PMID:
27647903
Author(s):
Sawaya, M.R., Rodriguez, J., Cascio, D., Collazo, M.J., Shi, D., Reyes, F.E., Hattne, J., Gonen, T., Eisenberg, D.S.
Reference:
Proc Natl Acad Sci U S A. 2016 Oct 4;113(40):11232-11236. Epub 2016 Sep 19
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Entry:
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Structure:
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Protein Information
Protein Name:
Eukaryotic peptide chain release factor GTP-binding subunit
Alternative Name:
Gene Name:
Sequence Length:
6
Species:
Saccharomyces cerevisiae
Mutation(s):
No
E.C. Number:
UniProt ID:
P05453
Keyword(s):
Eukaryotic peptide chain release factor GTP-binding subunit
Structure Information
PDB ID:
5K2F
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
Homo 18-mer - A18
PDB Classification:
PROTEIN FIBRIL
Method:
ELECTRON CRYSTALLOGRAPHY
Resolution (
Å
):
1.0
R free:
0.242
Ligand Information
Ligand ID
Chain ID
Ligand Formula
Ligand MW
Ligand Name
Ligand SMILES
InChI Key
ACT
A
C2 H3 O2 -1
59.04
ACETATE ION
CC(=O)[O-]
QTBSBXVTEAMEQO-UHFFFAOYSA-M
CD
A
Cd 2
112.41
CADMIUM ION
[Cd+2]
WLZRMCYVCSSEQC-UHFFFAOYSA-N
Entry:S-0435
PDB ID: 5K2G
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Sequence & Sec. Str.
Chain 1
1
G
N
N
Q
Q
N
Y
7
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Structure of GNNQQNY from yeast prion Sup35 in space group P21 determined by MicroED
They show with four structures of the amyloid core of the Sup35 prion protein that, if the diffraction resolution is high enough, sufficiently accurate phases can be obtained by direct methods with the cryo-EM method microelectron diffraction (MicroED), just as in X-ray diffraction.
Literature
PMID:
27647903
Author(s):
Sawaya, M.R., Rodriguez, J., Cascio, D., Collazo, M.J., Shi, D., Reyes, F.E., Hattne, J., Gonen, T., Eisenberg, D.S.
Reference:
Proc Natl Acad Sci U S A. 2016 Oct 4;113(40):11232-11236. Epub 2016 Sep 19
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Protein Information
Protein Name:
Eukaryotic peptide chain release factor GTP-binding subunit
Alternative Name:
Gene Name:
Sequence Length:
7
Species:
Saccharomyces cerevisiae
Mutation(s):
No
E.C. Number:
UniProt ID:
P05453
Keyword(s):
Eukaryotic peptide chain release factor GTP-binding subunit
Structure Information
PDB ID:
5K2G
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
Homo 18-mer - A18
PDB Classification:
PROTEIN FIBRIL
Method:
ELECTRON CRYSTALLOGRAPHY
Resolution (
Å
):
1.1
R free:
0.22399999
Entry:S-0436
PDB ID: 5K2H
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Sequence & Sec. Str.
Chain 1
1
G
N
N
Q
Q
N
Y
7
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Structure of GNNQQNY from yeast prion Sup35 in space group P212121 determined by MicroED
They show with four structures of the amyloid core of the Sup35 prion protein that, if the diffraction resolution is high enough, sufficiently accurate phases can be obtained by direct methods with the cryo-EM method microelectron diffraction (MicroED), just as in X-ray diffraction.
Literature
PMID:
27647903
Author(s):
Sawaya, M.R., Rodriguez, J., Cascio, D., Collazo, M.J., Shi, D., Reyes, F.E., Hattne, J., Gonen, T., Eisenberg, D.S.
Reference:
Proc Natl Acad Sci U S A. 2016 Oct 4;113(40):11232-11236. Epub 2016 Sep 19
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Protein Information
Protein Name:
Eukaryotic peptide chain release factor GTP-binding subunit
Alternative Name:
Gene Name:
Sequence Length:
7
Species:
Saccharomyces cerevisiae
Mutation(s):
No
E.C. Number:
UniProt ID:
P05453
Keyword(s):
Eukaryotic peptide chain release factor GTP-binding subunit
Structure Information
PDB ID:
5K2H
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
Homo 18-mer - A18
PDB Classification:
PROTEIN FIBRIL
Method:
ELECTRON CRYSTALLOGRAPHY
Resolution (
Å
):
1.05
R free:
0.18600000
Entry:S-0437
PDB ID: 5K7N
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Sequence & Sec. Str.
Chain 1
1
V
Q
I
V
Y
K
6
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
MicroED structure of tau VQIVYK peptide at 1.1 A resolution
They show that fragmentation of large, imperfect crystals into microcrystals or nanocrystals can provide a simple path for high-resolution structure determination by the cryoEM method MicroED and potentially by serial femtosecond crystallography.
Literature
PMID:
28192420
Author(s):
de la Cruz, M.J., Hattne, J., Shi, D., Seidler, P., Rodriguez, J., Reyes, F.E., Sawaya, M.R., Cascio, D., Weiss, S.C., Kim, S.K., Hinck, C.S., Hinck, A.P., Calero, G., Eisenberg, D., Gonen, T.
Reference:
Nat Methods. 2017 Feb 13;14(4):399-402.
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Protein Information
Protein Name:
Microtubule-associated protein tau
Alternative Name:
Gene Name:
Sequence Length:
6
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
P10636
Keyword(s):
VQIVYK
Structure Information
PDB ID:
5K7N
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
Homo 9-mer - A9
PDB Classification:
PROTEIN FIBRIL
Method:
ELECTRON CRYSTALLOGRAPHY
Resolution (
Å
):
1.1
R free:
0.223
Entry:S-0438
PDB ID: 5KK3
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Sequence & Sec. Str.
Chain 1
1
D
A
E
F
R
H
D
S
G
Y
E
V
H
H
Q
K
L
V
F
F
A
E
D
V
G
25
26
S
N
K
G
A
I
I
G
L
M
V
G
G
V
V
I
A
42
Chain 2
1
D
A
E
F
R
H
D
S
G
Y
E
V
H
H
Q
K
L
V
F
F
A
E
D
V
G
25
26
S
N
K
G
A
I
I
G
L
M
V
G
G
V
V
I
A
42
Chain 3
1
D
A
E
F
R
H
D
S
G
Y
E
V
H
H
Q
K
L
V
F
F
A
E
D
V
G
25
26
S
N
K
G
A
I
I
G
L
M
V
G
G
V
V
I
A
42
Chain 4
1
D
A
E
F
R
H
D
S
G
Y
E
V
H
H
Q
K
L
V
F
F
A
E
D
V
G
25
26
S
N
K
G
A
I
I
G
L
M
V
G
G
V
V
I
A
42
Chain 5
1
D
A
E
F
R
H
D
S
G
Y
E
V
H
H
Q
K
L
V
F
F
A
E
D
V
G
25
26
S
N
K
G
A
I
I
G
L
M
V
G
G
V
V
I
A
42
Chain 6
1
D
A
E
F
R
H
D
S
G
Y
E
V
H
H
Q
K
L
V
F
F
A
E
D
V
G
25
26
S
N
K
G
A
I
I
G
L
M
V
G
G
V
V
I
A
42
Chain 7
1
D
A
E
F
R
H
D
S
G
Y
E
V
H
H
Q
K
L
V
F
F
A
E
D
V
G
25
26
S
N
K
G
A
I
I
G
L
M
V
G
G
V
V
I
A
42
Chain 8
1
D
A
E
F
R
H
D
S
G
Y
E
V
H
H
Q
K
L
V
F
F
A
E
D
V
G
25
26
S
N
K
G
A
I
I
G
L
M
V
G
G
V
V
I
A
42
Chain 9
1
D
A
E
F
R
H
D
S
G
Y
E
V
H
H
Q
K
L
V
F
F
A
E
D
V
G
25
26
S
N
K
G
A
I
I
G
L
M
V
G
G
V
V
I
A
42
Chain 10
1
D
A
E
F
R
H
D
S
G
Y
E
V
H
H
Q
K
L
V
F
F
A
E
D
V
G
25
26
S
N
K
G
A
I
I
G
L
M
V
G
G
V
V
I
A
42
Chain 11
1
D
A
E
F
R
H
D
S
G
Y
E
V
H
H
Q
K
L
V
F
F
A
E
D
V
G
25
26
S
N
K
G
A
I
I
G
L
M
V
G
G
V
V
I
A
42
Chain 12
1
D
A
E
F
R
H
D
S
G
Y
E
V
H
H
Q
K
L
V
F
F
A
E
D
V
G
25
26
S
N
K
G
A
I
I
G
L
M
V
G
G
V
V
I
A
42
Chain 13
1
D
A
E
F
R
H
D
S
G
Y
E
V
H
H
Q
K
L
V
F
F
A
E
D
V
G
25
26
S
N
K
G
A
I
I
G
L
M
V
G
G
V
V
I
A
42
Chain 14
1
D
A
E
F
R
H
D
S
G
Y
E
V
H
H
Q
K
L
V
F
F
A
E
D
V
G
25
26
S
N
K
G
A
I
I
G
L
M
V
G
G
V
V
I
A
42
Chain 15
1
D
A
E
F
R
H
D
S
G
Y
E
V
H
H
Q
K
L
V
F
F
A
E
D
V
G
25
26
S
N
K
G
A
I
I
G
L
M
V
G
G
V
V
I
A
42
Chain 16
1
D
A
E
F
R
H
D
S
G
Y
E
V
H
H
Q
K
L
V
F
F
A
E
D
V
G
25
26
S
N
K
G
A
I
I
G
L
M
V
G
G
V
V
I
A
42
Chain 17
1
D
A
E
F
R
H
D
S
G
Y
E
V
H
H
Q
K
L
V
F
F
A
E
D
V
G
25
26
S
N
K
G
A
I
I
G
L
M
V
G
G
V
V
I
A
42
Chain 18
1
D
A
E
F
R
H
D
S
G
Y
E
V
H
H
Q
K
L
V
F
F
A
E
D
V
G
25
26
S
N
K
G
A
I
I
G
L
M
V
G
G
V
V
I
A
42
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Atomic Resolution Structure of Monomorphic AB42 Amyloid Fibrils
They present an atomic resolution structure of a monomorphic form of ABetaM01-42 amyloid fibrils. The structure shows that the fibril core consists of a dimer of ABeta42 molecules, each containing four Beta-strands in a S-shaped amyloid fold, and arranged in a manner that generates two hydrophobic cores that are capped at the end of the chain by a salt bridge. The outer surface of the monomers presents hydrophilic side chains to the solvent. The interface between the monomers of the dimer shows clear contacts between M35 of one molecule and L17 and Q15 of the second. Intermolecular (13)C-(15)N constraints demonstrate that the amyloid fibrils are parallel in register.
Literature
PMID:
27355699
Author(s):
Colvin, M.T., Silvers, R., Ni, Q.Z., Can, T.V., Sergeyev, I., Rosay, M., Donovan, K.J., Michael, B., Wall, J., Linse, S., Griffin, R.G.
Reference:
J Am Chem Soc. 2016 Aug 3;138(30):9663-74.
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Protein Information
Protein Name:
Amyloid-beta A4 protein
Alternative Name:
ABPP, APPI, Alzheimer disease amyloid protein, Amyloid precursor protein, Amyloid-beta precursor protein, Cerebral vascular amyloid peptide, PreA4, Protease nexin-II
Gene Name:
APP, A4, AD1
Sequence Length:
42
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
P05067
Keyword(s):
Beta-amyloid protein 42
Structure Information
PDB ID:
5KK3
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
Homo 18-mer - A18
PDB Classification:
PROTEIN FIBRIL
Method:
SOLID-STATE NMR
Resolution (
Å
):
R free:
Entry:S-0439
PDB ID: 5KNZ
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Sequence & Sec. Str.
Chain 1
1
S
G
N
N
F
G
A
I
L
S
S
11
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Human Islet Amyloid Polypeptide Segment 19-SGNNFGAILSS-29 with Early Onset S20G Mutation Determined by MicroED
Human Islet Amyloid Polypeptide Segment 19-SGNNFGAILSS-29 with Early Onset S20G Mutation Determined by MicroED
Literature
PMID:
Author(s):
Krotee, P.A.L., Rodriguez, J.A., Sawaya, M.R., Cascio, D., Reyes, F.E., Shi, D., Hattne, J., Nannenga, B.L., Oskarsson, M., Griner, S., Jiang, L., Westermark, G., Gonen, T., Eisenberg, D.S.
Reference:
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Entry:
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Protein Information
Protein Name:
Islet amyloid polypeptide
Alternative Name:
Gene Name:
Sequence Length:
11
Species:
Homo sapiens
Mutation(s):
S20G
E.C. Number:
UniProt ID:
P10997
Keyword(s):
hIAPP(residues 19-29)S20G
Structure Information
PDB ID:
5KNZ
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
Homo 18-mer - A18
PDB Classification:
PROTEIN FIBRIL
Method:
ELECTRON CRYSTALLOGRAPHY
Resolution (
Å
):
1.9
R free:
0.275
Entry:S-0440
PDB ID: 5KO0
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Sequence & Sec. Str.
Chain 1
1
F
L
V
H
S
S
N
N
F
G
A
11
Chain 2
1
F
L
V
H
S
S
N
N
F
G
A
11
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Human Islet Amyloid Polypeptide Segment 15-FLVHSSNNFGA-25 Determined by MicroED
Human Islet Amyloid Polypeptide Segment 15-FLVHSSNNFGA-25 Determined by MicroED
Literature
PMID:
Author(s):
Krotee, P.A.L., Rodriguez, J.A., Sawaya, M.R., Cascio, D., Reyes, F.E., Shi, D., Hattne, J., Nannenga, B.L., Oskarsson, M., Griner, S., Jiang, L., Westermark, G., Gonen, T., Eisenberg, D.S.
Reference:
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Entry:
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Structure:
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Contact Network:
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Protein Information
Protein Name:
Islet amyloid polypeptide
Alternative Name:
Gene Name:
Sequence Length:
11
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
P10997
Keyword(s):
hIAPP(15-25)WT
Structure Information
PDB ID:
5KO0
Amyloid Category:
Amyloid
Type:
Fibril
Global Stoichiometry:
Homo 18-mer - A18
PDB Classification:
PROTEIN FIBRIL
Method:
ELECTRON CRYSTALLOGRAPHY
Resolution (
Å
):
1.4
R free:
0.259
Ligand Information
Ligand ID
Chain ID
Ligand Formula
Ligand MW
Ligand Name
Ligand SMILES
InChI Key
SCN
B
C N S -1
58.08
THIOCYANATE ION
C(#N)[S-]
ZMZDMBWJUHKJPS-UHFFFAOYSA-M
Entry:S-0441
PDB ID: 5L6Q
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Protein Contacts Atlas
Sequence & Sec. Str.
Chain 1
1
S
E
L
T
Q
D
P
A
V
S
V
A
L
G
Q
T
V
R
I
T
C
Q
G
D
S
25
26
L
R
S
Y
S
A
S
W
Y
Q
Q
K
P
G
Q
A
P
V
L
V
I
F
R
K
S
50
51
N
R
P
S
G
I
P
D
R
F
S
G
S
S
S
G
N
T
A
S
L
T
I
T
G
75
76
A
Q
A
E
D
E
A
D
Y
Y
C
N
S
R
D
S
S
A
N
H
Q
V
F
G
G
100
101
G
T
K
L
T
V
L
G
Q
P
K
A
A
P
S
115
Chain 2
1
S
E
L
T
Q
D
P
A
V
S
V
A
L
G
Q
T
V
R
I
T
C
Q
G
D
S
25
26
L
R
S
Y
S
A
S
W
Y
Q
Q
K
P
G
Q
A
P
V
L
V
I
F
R
K
S
50
51
N
R
P
S
G
I
P
D
R
F
S
G
S
S
S
G
N
T
A
S
L
T
I
T
G
75
76
A
Q
A
E
D
E
A
D
Y
Y
C
N
S
R
D
S
S
A
N
H
Q
V
F
G
G
100
101
G
T
K
L
T
V
L
G
Q
P
K
A
A
P
S
115
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Refolded AL protein from cardiac amyloidosis
Chemical and biophysical analysis of amyloid fibrils from human AL and murine AA amyloidosis reveal the same fibril morphologies in different tissues or organs of one patient or diseased animal. The observed structural similarities concerned the fibril morphology, the fibril protein primary and secondary structures, the presence of post-translational modifications and, in case of the AL fibrils, the partially folded characteristics of the polypeptide chain within the fibril. The structure is Refolded AL protein from cardiac amyloidosis
Literature
PMID:
28544119
Author(s):
Annamalai, K., Liberta, F., Vielberg, M.T., Close, W., Lilie, H., Guhrs, K.H., Schierhorn, A., Koehler, R., Schmidt, A., Haupt, C., Hegenbart, U., Schonland, S., Schmidt, M., Groll, M., Fandrich, M.
Reference:
Angew Chem Int Ed Engl. 2017 Jun 19;56(26):7510-7514.
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Protein Information
Protein Name:
AL protein
Alternative Name:
Gene Name:
Sequence Length:
115
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
Keyword(s):
H5AL
Structure Information
PDB ID:
5L6Q
Amyloid Category:
Amyloid
Type:
Protein
Global Stoichiometry:
Homo 2-mer -A2
PDB Classification:
IMMUNE SYSTEM
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
1.4
R free:
0.182
Ligand Information
Ligand ID
Chain ID
Ligand Formula
Ligand MW
Ligand Name
Ligand SMILES
InChI Key
CO3
A
C O3 -2
60.01
CARBONATE ION
C(=O)([O-])[O-]
BVKZGUZCCUSVTD-UHFFFAOYSA-L
nan
A
Na 1
22.99
SODIUM ION
[Na+]
FKNQFGJONOIPTF-UHFFFAOYSA-N
PEG
A
C4 H10 O3
106.12
DI(HYDROXYETHYL)ETHER
C(COCCO)O
MTHSVFCYNBDYFN-UHFFFAOYSA-N
ZN
A
Zn 2
65.41
ZINC ION
[Zn+2]
PTFCDOFLOPIGGS-UHFFFAOYSA-N
CL
B
Cl -1
35.45
CHLORIDE ION
[Cl-]
VEXZGXHMUGYJMC-UHFFFAOYSA-M
CO3
B
C O3 -2
60.01
CARBONATE ION
C(=O)([O-])[O-]
BVKZGUZCCUSVTD-UHFFFAOYSA-L
nan
B
Na 1
22.99
SODIUM ION
[Na+]
FKNQFGJONOIPTF-UHFFFAOYSA-N
PGE
B
C6 H14 O4
150.17
TRIETHYLENE GLYCOL
C(COCCOCCO)O
ZIBGPFATKBEMQZ-UHFFFAOYSA-N
ZN
B
Zn 2
65.41
ZINC ION
[Zn+2]
PTFCDOFLOPIGGS-UHFFFAOYSA-N
Entry:S-0442
PDB ID: 5L6R
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Structure
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Sequence & Sec. Str.
Chain 1
1
G
Q
G
G
G
T
H
S
Q
W
N
K
P
S
K
P
K
T
N
M
K
H
M
A
G
25
26
A
A
A
A
G
A
V
V
G
G
L
G
G
Y
M
L
G
S
A
M
S
R
P
I
I
50
51
H
F
G
S
D
Y
E
D
R
Y
Y
R
E
N
M
H
R
Y
P
N
Q
V
Y
Y
R
75
76
P
M
D
E
Y
S
N
Q
N
N
F
V
H
D
C
V
N
I
T
I
K
Q
H
T
V
100
101
T
T
T
T
K
G
E
N
F
T
E
T
D
V
K
M
M
E
R
V
V
E
Q
M
C
125
126
I
T
Q
Y
E
R
E
S
Q
A
Y
Y
G
G
H
H
H
H
H
H
145
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
PrP226* - Solution-state NMR structure of truncated human prion protein
They have determined the NMR structure of recombinant PrP226. The structure of the protein consists of a disordered N-terminal part (residues 90-125) and a structured C-terminal part (residues 126-226). The C-terminal segment consists of four Alpha-helices and a short antiparallel Beta-sheet. Our model predicts a break in the C-terminal helix and reorganized hydrophobic interactions between helix Alpha 3 and Beta 2 -Alpha 2 loop due to the shorter C-terminus.
Literature
PMID:
28109886
Author(s):
Kovac, V., Zupancic, B., Ilc, G., Plavec, J., Curin Serbec, V.
Reference:
Biochem Biophys Res Commun. 2017 Feb 26;484(1):45-50.
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Protein Information
Protein Name:
Major prion protein
Alternative Name:
ASCR, PrP27-30, PrP33-35C
Gene Name:
PRNP, ALTPRP, PRIP, PRP
Sequence Length:
145
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
P04156
Keyword(s):
Major prion protein
Structure Information
PDB ID:
5L6R
Amyloid Category:
Amyloid
Type:
Protein
Global Stoichiometry:
Monomer - A
PDB Classification:
TRANSPORT PROTEIN
Method:
SOLUTION NMR
Resolution (
Å
):
R free:
Entry:S-0443
PDB ID: 5LFY
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Sequence & Sec. Str.
Chain 1
1
D
A
E
F
R
H
H
S
G
Y
X
11
Chain 2
1
D
A
E
F
R
H
H
S
G
Y
X
11
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Zinc bound dimer of the fragment of human amyloid-beta peptide with Alzheimer's disease pathogenic Taiwanese mutation D7H
Mutations and modifications in the metal binding domain 1-16 of ABeta peptide crucially affect its zinc-induced oligomerization by changing intermolecular zinc mediated interface. The 3D structure of this interface appearing in a range of ABeta species is a prospective drug target for disease modifying therapy. The interaction of zinc ions with ABeta fragments 1-7 and 1-10 carrying familial Taiwanese mutation D7H was studied. Zinc ions induce formation of a stable homodimer formed by the two peptide chains fastened by two zinc ions and stacking interactions of imidazole rings. A binuclear zinc interaction fold in the dimer structure was discovered.
Literature
PMID:
28570778
Author(s):
Polshakov, V.I., Mantsyzov, A.B., Kozin, S.A., Adzhubei, A.A., Zhokhov, S.S., van Beek, W., Kulikova, A.A., Indeykina, M.I., Mitkevich, V.A., Makarov, A.A.
Reference:
Angew Chem Int Ed Engl. 2017 Sep 18;56(39):11734-11739.
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Structure:
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Contact Network:
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Protein Information
Protein Name:
Amyloid-beta A4 protein
Alternative Name:
Gene Name:
Sequence Length:
11
Species:
Homo sapiens
Mutation(s):
D7H
E.C. Number:
UniProt ID:
P05067
Keyword(s):
Amyloid beta A4 protein
Structure Information
PDB ID:
5LFY
Amyloid Category:
Amyloid
Type:
Peptide
Global Stoichiometry:
Homo 2-mer -A2
PDB Classification:
STRUCTURAL PROTEIN
Method:
SOLUTION NMR
Resolution (
Å
):
R free:
Ligand Information
Ligand ID
Chain ID
Ligand Formula
Ligand MW
Ligand Name
Ligand SMILES
InChI Key
NH2
A
H2 N
16.02
AMINO GROUP
[NH2]
QGZKDVFQNNGYKY-UHFFFAOYAF
ZN
A
Zn 2
65.41
ZINC ION
[Zn+2]
PTFCDOFLOPIGGS-UHFFFAOYSA-N
NH2
B
H2 N
16.02
AMINO GROUP
[NH2]
QGZKDVFQNNGYKY-UHFFFAOYAF
Entry:S-0444
PDB ID: 5M6A
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Structure
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Protein Contacts Atlas
Sequence & Sec. Str.
Chain 1
1
Q
S
A
L
T
Q
P
P
S
A
S
G
S
P
G
Q
S
V
T
I
S
C
T
G
T
25
26
S
S
D
V
G
G
S
D
S
V
S
W
Y
Q
Q
H
P
G
K
A
P
K
L
I
I
50
51
Y
E
V
S
Q
R
P
S
G
V
P
N
R
F
S
G
S
K
S
G
N
T
A
S
L
75
76
T
V
S
G
L
Q
A
E
D
D
A
D
Y
Y
C
S
S
Y
G
G
D
N
N
L
F
100
101
F
G
G
G
T
K
V
T
V
L
G
Q
P
K
A
A
P
S
V
T
L
F
P
P
S
125
126
S
E
E
L
Q
A
N
K
A
T
L
V
C
L
I
S
D
F
Y
P
G
A
V
T
V
150
151
A
W
K
A
D
S
S
P
V
K
A
G
V
E
T
T
T
P
S
K
Q
S
N
N
K
175
176
Y
A
A
S
S
Y
L
S
L
T
P
E
Q
W
K
S
H
R
S
Y
S
C
Q
V
T
200
201
H
E
G
S
T
V
E
K
T
V
A
P
T
E
C
S
216
Chain 2
1
Q
S
A
L
T
Q
P
P
S
A
S
G
S
P
G
Q
S
V
T
I
S
C
T
G
T
25
26
S
S
D
V
G
G
S
D
S
V
S
W
Y
Q
Q
H
P
G
K
A
P
K
L
I
I
50
51
Y
E
V
S
Q
R
P
S
G
V
P
N
R
F
S
G
S
K
S
G
N
T
A
S
L
75
76
T
V
S
G
L
Q
A
E
D
D
A
D
Y
Y
C
S
S
Y
G
G
D
N
N
L
F
100
101
F
G
G
G
T
K
V
T
V
L
G
Q
P
K
A
A
P
S
V
T
L
F
P
P
S
125
126
S
E
E
L
Q
A
N
K
A
T
L
V
C
L
I
S
D
F
Y
P
G
A
V
T
V
150
151
A
W
K
A
D
S
S
P
V
K
A
G
V
E
T
T
T
P
S
K
Q
S
N
N
K
175
176
Y
A
A
S
S
Y
L
S
L
T
P
E
Q
W
K
S
H
R
S
Y
S
C
Q
V
T
200
201
H
E
G
S
T
V
E
K
T
V
A
P
T
E
C
S
216
Chain 3
1
Q
S
A
L
T
Q
P
P
S
A
S
G
S
P
G
Q
S
V
T
I
S
C
T
G
T
25
26
S
S
D
V
G
G
S
D
S
V
S
W
Y
Q
Q
H
P
G
K
A
P
K
L
I
I
50
51
Y
E
V
S
Q
R
P
S
G
V
P
N
R
F
S
G
S
K
S
G
N
T
A
S
L
75
76
T
V
S
G
L
Q
A
E
D
D
A
D
Y
Y
C
S
S
Y
G
G
D
N
N
L
F
100
101
F
G
G
G
T
K
V
T
V
L
G
Q
P
K
A
A
P
S
V
T
L
F
P
P
S
125
126
S
E
E
L
Q
A
N
K
A
T
L
V
C
L
I
S
D
F
Y
P
G
A
V
T
V
150
151
A
W
K
A
D
S
S
P
V
K
A
G
V
E
T
T
T
P
S
K
Q
S
N
N
K
175
176
Y
A
A
S
S
Y
L
S
L
T
P
E
Q
W
K
S
H
R
S
Y
S
C
Q
V
T
200
201
H
E
G
S
T
V
E
K
T
V
A
P
T
E
C
S
216
Chain 4
1
Q
S
A
L
T
Q
P
P
S
A
S
G
S
P
G
Q
S
V
T
I
S
C
T
G
T
25
26
S
S
D
V
G
G
S
D
S
V
S
W
Y
Q
Q
H
P
G
K
A
P
K
L
I
I
50
51
Y
E
V
S
Q
R
P
S
G
V
P
N
R
F
S
G
S
K
S
G
N
T
A
S
L
75
76
T
V
S
G
L
Q
A
E
D
D
A
D
Y
Y
C
S
S
Y
G
G
D
N
N
L
F
100
101
F
G
G
G
T
K
V
T
V
L
G
Q
P
K
A
A
P
S
V
T
L
F
P
P
S
125
126
S
E
E
L
Q
A
N
K
A
T
L
V
C
L
I
S
D
F
Y
P
G
A
V
T
V
150
151
A
W
K
A
D
S
S
P
V
K
A
G
V
E
T
T
T
P
S
K
Q
S
N
N
K
175
176
Y
A
A
S
S
Y
L
S
L
T
P
E
Q
W
K
S
H
R
S
Y
S
C
Q
V
T
200
201
H
E
G
S
T
V
E
K
T
V
A
P
T
E
C
S
216
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Crystal structure of cardiotoxic Bence-Jones light chain dimer H9
Eight amyloidogenic LCs were selected as responsible for severe cardiac symptoms in patients; five non-amyloidogenic LCs were isolated from patients affected by multiple myeloma. They showed that low fold stability and high protein dynamics correlate with amyloidogenic LCs, while hydrophobicity, structural rearrangements and nature of the LC dimeric association interface do not appear to play a significant role in defining amyloid propensity.
Literature
PMID:
29196671
Author(s):
Oberti, L., Rognoni, P., Barbiroli, A., Lavatelli, F., Russo, R., Maritan, M., Palladini, G., Bolognesi, M., Merlini, G., Ricagno, S.
Reference:
Sci Rep. 2017 Dec 1;7(1):16809.
Download
Entry:
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Structure:
PDB
CIF
FASTA
Contact Network:
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Protein Information
Protein Name:
Bence-Jones light chain dimer H9
Alternative Name:
Gene Name:
Sequence Length:
216
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
Keyword(s):
Bence-Jones light chain
Structure Information
PDB ID:
5M6A
Amyloid Category:
Amyloid
Type:
Protein
Global Stoichiometry:
Homo 2-mer - A2
PDB Classification:
IMMUNE SYSTEM
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
1.64
R free:
0.203
Ligand Information
Ligand ID
Chain ID
Ligand Formula
Ligand MW
Ligand Name
Ligand SMILES
InChI Key
GOL
A
C3 H8 O3
92.09
GLYCEROL
C(C(CO)O)O
PEDCQBHIVMGVHV-UHFFFAOYSA-N
PO4
A
O4 P -3
94.97
PHOSPHATE ION
[O-]P(=O)([O-])[O-]
NBIIXXVUZAFLBC-UHFFFAOYSA-K
GOL
B
C3 H8 O3
92.09
GLYCEROL
C(C(CO)O)O
PEDCQBHIVMGVHV-UHFFFAOYSA-N
PO4
B
O4 P -3
94.97
PHOSPHATE ION
[O-]P(=O)([O-])[O-]
NBIIXXVUZAFLBC-UHFFFAOYSA-K
GOL
C
C3 H8 O3
92.09
GLYCEROL
C(C(CO)O)O
PEDCQBHIVMGVHV-UHFFFAOYSA-N
GOL
D
C3 H8 O3
92.09
GLYCEROL
C(C(CO)O)O
PEDCQBHIVMGVHV-UHFFFAOYSA-N
PO4
D
O4 P -3
94.97
PHOSPHATE ION
[O-]P(=O)([O-])[O-]
NBIIXXVUZAFLBC-UHFFFAOYSA-K
Entry:S-0445
PDB ID: 5M6I
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Structure
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Protein Contacts Atlas
Sequence & Sec. Str.
Chain 1
1
E
S
A
L
T
Q
P
A
S
V
S
G
S
P
G
Q
S
I
T
I
S
C
T
G
T
25
26
S
S
D
V
G
A
Y
N
L
V
S
W
Y
Q
Q
H
P
G
K
T
P
K
L
L
I
50
51
Y
E
V
S
K
R
P
S
G
V
S
N
R
F
S
G
S
K
S
G
N
T
A
S
L
75
76
T
I
S
G
L
Q
P
E
D
E
A
D
Y
Y
C
C
S
N
A
G
S
Y
T
H
V
100
101
F
G
T
G
T
K
V
T
V
L
V
Q
P
K
A
N
P
T
V
T
L
F
P
P
S
125
126
S
E
E
L
Q
A
N
K
A
T
L
V
C
L
I
S
D
F
Y
P
G
A
V
T
V
150
151
A
W
K
A
D
G
S
P
V
K
A
G
V
E
T
T
K
P
S
K
Q
S
N
N
K
175
176
Y
A
A
S
S
Y
L
S
L
T
P
E
Q
W
K
S
H
R
S
Y
S
C
Q
V
T
200
201
H
E
G
S
T
V
E
K
T
V
A
P
T
E
C
S
216
Chain 2
1
Q
S
A
L
T
Q
P
A
S
V
S
G
S
P
G
Q
S
I
T
I
S
C
T
G
T
25
26
S
S
D
V
G
A
Y
N
L
V
S
W
Y
Q
Q
H
P
G
K
T
P
K
L
L
I
50
51
Y
E
V
S
K
R
P
S
G
V
S
N
R
F
S
G
S
K
S
G
N
T
A
S
L
75
76
T
I
S
G
L
Q
P
E
D
E
A
D
Y
Y
C
C
S
N
A
G
S
Y
T
H
V
100
101
F
G
T
G
T
K
V
T
V
L
V
Q
P
K
A
N
P
T
V
T
L
F
P
P
S
125
126
S
E
E
L
Q
A
N
K
A
T
L
V
C
L
I
S
D
F
Y
P
G
A
V
T
V
150
151
A
W
K
A
D
G
S
P
V
K
A
G
V
E
T
T
K
P
S
K
Q
S
N
N
K
175
176
Y
A
A
S
S
Y
L
S
L
T
P
E
Q
W
K
S
H
R
S
Y
S
C
Q
V
T
200
201
H
E
G
S
T
V
E
K
T
V
A
P
T
E
C
S
216
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Crystal structure of non-cardiotoxic Bence-Jones light chain dimer M8
Eight amyloidogenic LCs were selected as responsible for severe cardiac symptoms in patients; five non-amyloidogenic LCs were isolated from patients affected by multiple myeloma. They showed that low fold stability and high protein dynamics correlate with amyloidogenic LCs, while hydrophobicity, structural rearrangements and nature of the LC dimeric association interface do not appear to play a significant role in defining amyloid propensity.
Literature
PMID:
29196671
Author(s):
Oberti, L., Rognoni, P., Barbiroli, A., Lavatelli, F., Russo, R., Maritan, M., Palladini, G., Bolognesi, M., Merlini, G., Ricagno, S.
Reference:
Sci Rep. 2017 Dec 1;7(1):16809.
Download
Entry:
CSV
JSON
Structure:
PDB
CIF
FASTA
Contact Network:
CSV
JSON
Protein Information
Protein Name:
Bence-Jones light chain dimer M8
Alternative Name:
Gene Name:
Sequence Length:
216
Species:
Mutation(s):
No
E.C. Number:
UniProt ID:
Keyword(s):
Structure Information
PDB ID:
5M6I
Amyloid Category:
Non-amyloid
Type:
Protein
Global Stoichiometry:
Homo 2-mer - A2
PDB Classification:
IMMUNE SYSTEM
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
2.2
R free:
0.22699999
Ligand Information
Ligand ID
Chain ID
Ligand Formula
Ligand MW
Ligand Name
Ligand SMILES
InChI Key
nan
A
Na 1
22.99
SODIUM ION
[Na+]
FKNQFGJONOIPTF-UHFFFAOYSA-N
PCA
A
C5 H7 N O3
129.11
PYROGLUTAMIC ACID
C1CC(=O)N[C@@H]1C(=O)O
ODHCTXKNWHHXJC-VKHMYHEASA-N
Entry:S-0446
PDB ID: 5M76
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Structure
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Protein Contacts Atlas
Sequence & Sec. Str.
Chain 1
1
Q
S
A
L
T
Q
E
A
S
V
S
G
T
V
G
Q
K
V
T
L
S
C
T
G
N
25
26
T
N
N
I
G
S
Y
P
V
G
W
Y
Q
Q
I
S
H
G
P
P
K
T
V
M
F
50
51
G
N
S
L
P
S
G
I
P
D
R
F
S
G
S
K
S
G
T
T
A
S
L
T
I
75
76
S
G
L
Q
P
E
D
E
A
D
Y
Y
C
S
T
W
D
S
S
L
S
V
Q
V
I
100
101
G
G
G
T
K
V
T
V
L
G
Q
P
K
A
A
P
S
V
T
L
F
P
P
S
S
125
126
E
E
L
Q
A
N
K
A
T
L
V
C
L
I
S
D
F
Y
P
G
A
V
T
V
A
150
151
W
K
A
D
S
S
P
V
K
A
G
V
E
T
T
T
P
S
K
Q
S
N
N
K
Y
175
176
A
A
S
S
Y
L
S
L
T
P
E
Q
W
K
S
H
R
S
Y
S
C
Q
V
T
H
200
201
E
G
S
T
V
E
K
T
V
A
P
T
E
C
S
215
Chain 2
1
Q
S
A
L
T
Q
E
A
S
V
S
G
T
V
G
Q
K
V
T
L
S
C
T
G
N
25
26
T
N
N
I
G
S
Y
P
V
G
W
Y
Q
Q
I
S
H
G
P
P
K
T
V
M
F
50
51
G
N
S
L
P
S
G
I
P
D
R
F
S
G
S
K
S
G
T
T
A
S
L
T
I
75
76
S
G
L
Q
P
E
D
E
A
D
Y
Y
C
S
T
W
D
S
S
L
S
V
Q
V
I
100
101
G
G
G
T
K
V
T
V
L
G
Q
P
K
A
A
P
S
V
T
L
F
P
P
S
S
125
126
E
E
L
Q
A
N
K
A
T
L
V
C
L
I
S
D
F
Y
P
G
A
V
T
V
A
150
151
W
K
A
D
S
S
P
V
K
A
G
V
E
T
T
T
P
S
K
Q
S
N
N
K
Y
175
176
A
A
S
S
Y
L
S
L
T
P
E
Q
W
K
S
H
R
S
Y
S
C
Q
V
T
H
200
201
E
G
S
T
V
E
K
T
V
A
P
T
E
C
S
215
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Crystal structure of cardiotoxic Bence-Jones light chain dimer H10
Eight amyloidogenic LCs were selected as responsible for severe cardiac symptoms in patients; five non-amyloidogenic LCs were isolated from patients affected by multiple myeloma. They showed that low fold stability and high protein dynamics correlate with amyloidogenic LCs, while hydrophobicity, structural rearrangements and nature of the LC dimeric association interface do not appear to play a significant role in defining amyloid propensity.
Literature
PMID:
29196671
Author(s):
Oberti, L., Rognoni, P., Barbiroli, A., Lavatelli, F., Russo, R., Maritan, M., Palladini, G., Bolognesi, M., Merlini, G., Ricagno, S.
Reference:
Sci Rep. 2017 Dec 1;7(1):16809.
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Entry:
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Structure:
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Contact Network:
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JSON
Protein Information
Protein Name:
Bence-Jones light chain dimer H10
Alternative Name:
Gene Name:
Sequence Length:
215
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
Keyword(s):
light chain dimer
Structure Information
PDB ID:
5M76
Amyloid Category:
Amyloid
Type:
Protein
Global Stoichiometry:
Homo 2-mer - A2
PDB Classification:
IMMUNE SYSTEM
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
2.5
R free:
0.282
Ligand Information
Ligand ID
Chain ID
Ligand Formula
Ligand MW
Ligand Name
Ligand SMILES
InChI Key
BR
B
Br -1
79.9
BROMIDE ION
[Br-]
CPELXLSAUQHCOX-UHFFFAOYSA-M
Entry:S-0447
PDB ID: 5MGQ
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Structure
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Sequence & Sec. Str.
Chain 1
1
K
C
N
T
A
T
C
A
T
Q
R
L
A
N
F
L
V
H
S
S
N
N
F
G
A
25
26
I
L
S
S
T
N
V
G
S
N
T
X
37
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Solution structure of oxidized and amidated human IAPP (1-37), the diabetes II peptide.
They present a structural characterization of hIAPP in solution, demonstrating that the N-terminus of the oxidized peptide has a high propensity to form an Alpha-helical structure which is lacking in the reduced state of hIAPP. In healthy cells, this residual structure prevents the conversion into amyloidogenic aggregates.
Literature
PMID:
28287098
Author(s):
Rodriguez Camargo, D.C., Tripsianes, K., Buday, K., Franko, A., Gobl, C., Hartlmuller, C., Sarkar, R., Aichler, M., Mettenleiter, G., Schulz, M., Boddrich, A., Erck, C., Martens, H., Walch, A.K., Madl, T., Wanker, E.E., Conrad, M., de Angelis, M.H., Reif,
Reference:
Sci Rep. 2017 Mar 13;7:44041.
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Entry:
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Structure:
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Contact Network:
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Protein Information
Protein Name:
Islet amyloid polypeptide
Alternative Name:
Amylin, Diabetes-associated peptide, Insulinoma amyloid peptide
Gene Name:
IAPP
Sequence Length:
37
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
P10997
Keyword(s):
Islet amyloid polypeptide
Structure Information
PDB ID:
5MGQ
Amyloid Category:
Amyloid
Type:
Peptide
Global Stoichiometry:
Monomer - A
PDB Classification:
PROTEIN FIBRIL
Method:
SOLUTION NMR
Resolution (
Å
):
R free:
Ligand Information
Ligand ID
Chain ID
Ligand Formula
Ligand MW
Ligand Name
Ligand SMILES
InChI Key
TYC
A
C9 H12 N2 O2
180.2
L-TYROSINAMIDE
c1cc(ccc1C[C@@H](C(=O)N)N)O
PQFMNVGMJJMLAE-QMMMGPOBSA-N
Entry:S-0448
PDB ID: 5MTL
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Structure
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Protein Contacts Atlas
Sequence & Sec. Str.
Chain 1
1
Q
S
V
L
T
Q
P
P
S
T
S
G
T
P
G
Q
R
V
T
I
S
C
S
G
S
25
26
S
S
N
I
E
T
N
T
V
N
W
Y
Q
Q
L
P
G
T
A
P
K
L
V
M
H
50
51
T
N
N
Q
R
P
S
G
V
P
D
R
F
S
G
S
R
S
G
T
S
A
S
L
A
75
76
I
G
G
L
Q
S
E
D
E
A
D
Y
F
C
A
A
W
D
D
N
L
N
G
V
I
100
101
F
G
G
G
T
K
L
T
V
L
G
Q
P
K
A
A
P
S
V
T
L
F
P
P
S
125
126
S
E
E
L
Q
A
N
K
A
T
L
V
C
L
I
S
D
F
Y
P
G
A
V
T
V
150
151
A
W
K
A
D
S
S
P
V
K
A
G
V
E
T
T
T
P
S
K
Q
S
N
N
K
175
176
Y
A
A
S
S
Y
L
S
L
T
P
E
Q
W
K
S
H
K
S
Y
S
C
Q
V
T
200
201
H
E
G
S
T
V
E
K
T
V
A
P
T
E
C
S
216
Chain 2
1
Q
S
V
L
T
Q
P
P
S
T
S
G
T
P
G
Q
R
V
T
I
S
C
S
G
S
25
26
S
S
N
I
E
T
N
T
V
N
W
Y
Q
Q
L
P
G
T
A
P
K
L
V
M
H
50
51
T
N
N
Q
R
P
S
G
V
P
D
R
F
S
G
S
R
S
G
T
S
A
S
L
A
75
76
I
G
G
L
Q
S
E
D
E
A
D
Y
F
C
A
A
W
D
D
N
L
N
G
V
I
100
101
F
G
G
G
T
K
L
T
V
L
G
Q
P
K
A
A
P
S
V
T
L
F
P
P
S
125
126
S
E
E
L
Q
A
N
K
A
T
L
V
C
L
I
S
D
F
Y
P
G
A
V
T
V
150
151
A
W
K
A
D
S
S
P
V
K
A
G
V
E
T
T
T
P
S
K
Q
S
N
N
K
175
176
Y
A
A
S
S
Y
L
S
L
T
P
E
Q
W
K
S
H
K
S
Y
S
C
Q
V
T
200
201
H
E
G
S
T
V
E
K
T
V
A
P
T
E
C
S
216
Chain 3
1
Q
S
V
L
T
Q
P
P
S
T
S
G
T
P
G
Q
R
V
T
I
S
C
S
G
S
25
26
S
S
N
I
E
T
N
T
V
N
W
Y
Q
Q
L
P
G
T
A
P
K
L
V
M
H
50
51
T
N
N
Q
R
P
S
G
V
P
D
R
F
S
G
S
R
S
G
T
S
A
S
L
A
75
76
I
G
G
L
Q
S
E
D
E
A
D
Y
F
C
A
A
W
D
D
N
L
N
G
V
I
100
101
F
G
G
G
T
K
L
T
V
L
G
Q
P
K
A
A
P
S
V
T
L
F
P
P
S
125
126
S
E
E
L
Q
A
N
K
A
T
L
V
C
L
I
S
D
F
Y
P
G
A
V
T
V
150
151
A
W
K
A
D
S
S
P
V
K
A
G
V
E
T
T
T
P
S
K
Q
S
N
N
K
175
176
Y
A
A
S
S
Y
L
S
L
T
P
E
Q
W
K
S
H
K
S
Y
S
C
Q
V
T
200
201
H
E
G
S
T
V
E
K
T
V
A
P
T
E
C
S
216
Chain 4
1
Q
S
V
L
T
Q
P
P
S
T
S
G
T
P
G
Q
R
V
T
I
S
C
S
G
S
25
26
S
S
N
I
E
T
N
T
V
N
W
Y
Q
Q
L
P
G
T
A
P
K
L
V
M
H
50
51
T
N
N
Q
R
P
S
G
V
P
D
R
F
S
G
S
R
S
G
T
S
A
S
L
A
75
76
I
G
G
L
Q
S
E
D
E
A
D
Y
F
C
A
A
W
D
D
N
L
N
G
V
I
100
101
F
G
G
G
T
K
L
T
V
L
G
Q
P
K
A
A
P
S
V
T
L
F
P
P
S
125
126
S
E
E
L
Q
A
N
K
A
T
L
V
C
L
I
S
D
F
Y
P
G
A
V
T
V
150
151
A
W
K
A
D
S
S
P
V
K
A
G
V
E
T
T
T
P
S
K
Q
S
N
N
K
175
176
Y
A
A
S
S
Y
L
S
L
T
P
E
Q
W
K
S
H
K
S
Y
S
C
Q
V
T
200
201
H
E
G
S
T
V
E
K
T
V
A
P
T
E
C
S
216
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Crystal structure of an amyloidogenic light chain
Eight amyloidogenic LCs were selected as responsible for severe cardiac symptoms in patients; five non-amyloidogenic LCs were isolated from patients affected by multiple myeloma. They showed that low fold stability and high protein dynamics correlate with amyloidogenic LCs, while hydrophobicity, structural rearrangements and nature of the LC dimeric association interface do not appear to play a significant role in defining amyloid propensity.
Literature
PMID:
29196671
Author(s):
Oberti, L., Rognoni, P., Barbiroli, A., Lavatelli, F., Russo, R., Maritan, M., Palladini, G., Bolognesi, M., Merlini, G., Ricagno, S.
Reference:
Sci Rep. 2017 Dec 1;7(1):16809.
Download
Entry:
CSV
JSON
Structure:
PDB
CIF
FASTA
Contact Network:
CSV
JSON
Protein Information
Protein Name:
IGL@ protein
Alternative Name:
Gene Name:
IGL@
Sequence Length:
216
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
Q567P1
Keyword(s):
light chain dimer, IGL@ protein, IGL@ protein
Structure Information
PDB ID:
5MTL
Amyloid Category:
Amyloid
Type:
Protein
Global Stoichiometry:
Homo 2-mer - A2
PDB Classification:
IMMUNE SYSTEM
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
2.45
R free:
0.27699999
Entry:S-0449
PDB ID: 5MUD
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Structure
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Protein Contacts Atlas
Sequence & Sec. Str.
Chain 1
1
Q
S
V
L
T
Q
P
P
S
V
S
A
A
P
G
Q
K
V
T
I
S
C
S
G
N
25
26
N
S
N
I
G
K
N
Y
V
S
W
Y
Q
Q
L
P
G
R
T
P
K
V
I
M
Y
50
51
E
N
N
K
R
S
S
G
I
P
D
R
F
S
G
S
K
S
G
T
S
A
T
L
G
75
76
I
T
G
L
Q
T
G
D
E
A
D
Y
Y
C
G
V
W
D
S
S
L
S
G
G
V
100
101
F
G
G
G
T
K
V
T
V
L
G
Q
P
K
A
A
P
S
V
T
L
F
P
P
S
125
126
S
E
E
L
Q
A
N
K
A
T
L
V
C
L
I
S
D
F
Y
P
G
A
V
T
V
150
151
A
W
K
A
D
S
S
P
V
K
A
G
V
E
T
T
T
P
S
K
Q
S
N
N
K
175
176
Y
A
A
S
S
Y
L
S
L
T
P
E
Q
W
K
S
H
R
S
Y
S
C
Q
V
T
200
201
H
E
G
S
T
V
E
K
T
V
A
P
T
E
C
S
216
Chain 2
1
Q
S
V
L
T
Q
P
P
S
V
S
A
A
P
G
Q
K
V
T
I
S
C
S
G
N
25
26
N
S
N
I
G
K
N
Y
V
S
W
Y
Q
Q
L
P
G
R
T
P
K
V
I
M
Y
50
51
E
N
N
K
R
S
S
G
I
P
D
R
F
S
G
S
K
S
G
T
S
A
T
L
G
75
76
I
T
G
L
Q
T
G
D
E
A
D
Y
Y
C
G
V
W
D
S
S
L
S
G
G
V
100
101
F
G
G
G
T
K
V
T
V
L
G
Q
P
K
A
A
P
S
V
T
L
F
P
P
S
125
126
S
E
E
L
Q
A
N
K
A
T
L
V
C
L
I
S
D
F
Y
P
G
A
V
T
V
150
151
A
W
K
A
D
S
S
P
V
K
A
G
V
E
T
T
T
P
S
K
Q
S
N
N
K
175
176
Y
A
A
S
S
Y
L
S
L
T
P
E
Q
W
K
S
H
R
S
Y
S
C
Q
V
T
200
201
H
E
G
S
T
V
E
K
T
V
A
P
T
E
C
S
216
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Crystal structure of an amyloidogenic light chain dimer H6
Eight amyloidogenic LCs were selected as responsible for severe cardiac symptoms in patients; five non-amyloidogenic LCs were isolated from patients affected by multiple myeloma. They showed that low fold stability and high protein dynamics correlate with amyloidogenic LCs, while hydrophobicity, structural rearrangements and nature of the LC dimeric association interface do not appear to play a significant role in defining amyloid propensity.
Literature
PMID:
29196671
Author(s):
Oberti, L., Rognoni, P., Barbiroli, A., Lavatelli, F., Russo, R., Maritan, M., Palladini, G., Bolognesi, M., Merlini, G., Ricagno, S.
Reference:
Sci Rep. 2017 Dec 1;7(1):16809.
Download
Entry:
CSV
JSON
Structure:
PDB
CIF
FASTA
Contact Network:
CSV
JSON
Protein Information
Protein Name:
Immunoglobin light chain dimer H6
Alternative Name:
Gene Name:
Sequence Length:
216
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
Keyword(s):
light chain dimer, IGL@ protein
Structure Information
PDB ID:
5MUD
Amyloid Category:
Amyloid
Type:
Protein
Global Stoichiometry:
Homo 2-mer - A2
PDB Classification:
IMMUNE SYSTEM
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
2.34
R free:
0.249
Entry:S-0450
PDB ID: 5MUH
CSV
JSON
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Structure
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View interactive contact network
Protein Contacts Atlas
Sequence & Sec. Str.
Chain 1
1
Q
S
V
L
T
Q
P
P
S
V
S
A
A
P
G
Q
K
V
T
I
S
C
S
N
V
25
26
G
K
N
F
V
S
W
Y
Q
Q
F
P
G
T
A
P
K
V
V
I
Y
D
T
D
K
50
51
R
P
S
D
I
P
D
R
F
S
G
S
K
S
G
T
S
A
T
L
D
I
T
G
L
75
76
Q
T
G
D
E
A
D
Y
Y
C
G
T
W
D
S
G
L
N
G
G
V
F
G
G
G
100
101
T
K
V
T
V
L
G
Q
P
K
A
A
P
S
V
T
L
F
P
P
S
S
E
E
L
125
126
Q
A
N
K
A
T
L
V
C
L
I
S
D
F
Y
P
G
A
V
T
V
A
W
K
A
150
151
D
S
S
P
V
K
A
G
V
E
T
T
T
P
S
K
Q
S
N
N
K
Y
A
A
S
175
176
S
Y
L
S
L
T
P
E
Q
W
K
S
H
K
S
Y
S
C
Q
V
T
H
E
G
S
200
201
T
V
E
K
T
V
A
P
T
E
C
S
212
Chain 2
1
Q
S
V
L
T
Q
P
P
S
V
S
A
A
P
G
Q
K
V
T
I
S
C
S
N
V
25
26
G
K
N
F
V
S
W
Y
Q
Q
F
P
G
T
A
P
K
V
V
I
Y
D
T
D
K
50
51
R
P
S
D
I
P
D
R
F
S
G
S
K
S
G
T
S
A
T
L
D
I
T
G
L
75
76
Q
T
G
D
E
A
D
Y
Y
C
G
T
W
D
S
G
L
N
G
G
V
F
G
G
G
100
101
T
K
V
T
V
L
G
Q
P
K
A
A
P
S
V
T
L
F
P
P
S
S
E
E
L
125
126
Q
A
N
K
A
T
L
V
C
L
I
S
D
F
Y
P
G
A
V
T
V
A
W
K
A
150
151
D
S
S
P
V
K
A
G
V
E
T
T
T
P
S
K
Q
S
N
N
K
Y
A
A
S
175
176
S
Y
L
S
L
T
P
E
Q
W
K
S
H
K
S
Y
S
C
Q
V
T
H
E
G
S
200
201
T
V
E
K
T
V
A
P
T
E
C
S
212
Helix: Magenta; Strand: Yellow; Coil & Turn: White.
Charged residues and Proline are highlighed in blue.
Description
Crystal structure of an amyloidogenic light chain dimer H7
Eight amyloidogenic LCs were selected as responsible for severe cardiac symptoms in patients; five non-amyloidogenic LCs were isolated from patients affected by multiple myeloma. They showed that low fold stability and high protein dynamics correlate with amyloidogenic LCs, while hydrophobicity, structural rearrangements and nature of the LC dimeric association interface do not appear to play a significant role in defining amyloid propensity.
Literature
PMID:
29196671
Author(s):
Oberti, L., Rognoni, P., Barbiroli, A., Lavatelli, F., Russo, R., Maritan, M., Palladini, G., Bolognesi, M., Merlini, G., Ricagno, S.
Reference:
Sci Rep. 2017 Dec 1;7(1):16809.
Download
Entry:
CSV
JSON
Structure:
PDB
CIF
FASTA
Contact Network:
CSV
JSON
Protein Information
Protein Name:
Immunoglobin light chain dimer H7
Alternative Name:
Gene Name:
Sequence Length:
212
Species:
Homo sapiens
Mutation(s):
No
E.C. Number:
UniProt ID:
Keyword(s):
light chain dimer
Structure Information
PDB ID:
5MUH
Amyloid Category:
Amyloid
Type:
Protein
Global Stoichiometry:
Homo 2-mer - A2
PDB Classification:
IMMUNE SYSTEM
Method:
X-RAY DIFFRACTION
Resolution (
Å
):
2.65
R free:
0.266
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