{"reference": "J Biol Chem. 2015 Nov 27;290(48):28932-43.", "alternative_name": "ATTR, Prealbumin, TBPA", "entry": "S-0392", "gene_names": "TTR, PALB", "remarks": "Crystal Structure of Human Transthyretin Ser85Pro/Glu92Pro Mutant", "secondary_structure": "KCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGIPPFHEHAPVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKEHHHHHH#CCCEEEEEEETTTTEECTTCEEEEEEECTTSCEEEEEEEECCTTSEECCSCCTTTCCSEEEEEEECHHHHHHHHTCCCCEEEEEEEEEECCSSSCEEEEEEEEETTEEEEEEEEECCCCCCCCCC&KCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGIPPFHEHAPVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKEHHHHHH#CCCEEEEEEETTTTEECTTCEEEEEEECTTSCEEEEEEEECCTTSEECCSCCTTTCCSEEEEEEECHHHHHHHTTCCCSEEEEEEEEEESTTSCCEEEEEEEEETTEEEEEEEEECCCCCCCCCC", "chain_id": "A%%B%%B%%B", "inchi": "InChI=1S/Na/q+1%%InChI=1S/C3H8O3/c4-1-3(6)2-5/h3-6H,1-2H2%%InChI=1S/Na/q+1%%InChI=1S/C4H10O3/c5-1-3-7-4-2-6/h5-6H,1-4H2", "amyloid_non_amyloid": "Amyloid", "pmid": "26459562", "ligand_smiles": "[Na+]%%C(C(CO)O)O%%[Na+]%%C(COCCO)O", "keyword": "Transthyretin", "peptide_protein_sequence": "chain-ID A: KCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGIPPFHEHAPVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKEHHHHHH; chain-ID B: KCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGIPPFHEHAPVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKEHHHHHH", "uniprot_ac": "P02766", "protein_name": "Transthyretin", "r_value_free": "0.201", "mutation_s_field": "S85P/E92P", "ligand_mw": "22.99%%92.09%%22.99%%106.12", "pdb_id": "4TLK", "inchi_key": "FKNQFGJONOIPTF-UHFFFAOYSA-N%%PEDCQBHIVMGVHV-UHFFFAOYSA-N%%FKNQFGJONOIPTF-UHFFFAOYSA-N%%MTHSVFCYNBDYFN-UHFFFAOYSA-N", "ec_number": "", "pdb_classification": "TRANSPORT PROTEIN", "type": "Protein", "author": "Saelices, L., Johnson, L.M., Liang, W.Y., Sawaya, M.R., Cascio, D., Ruchala, P., Whitelegge, J., Jiang, L., Riek, R., Eisenberg, D.S.", "species": "Homo sapiens", "ligand_id": "nan%%GOL%%nan%%PEG", "method": "X-RAY DIFFRACTION", "ligand_name": "SODIUM ION%%GLYCEROL%%SODIUM ION%%DI(HYDROXYETHYL)ETHER", "global_stoichiometry": "Homo 4-mer - A4 ", "resolution": "1.44", "ligand_formula": "Na 1%%C3 H8 O3%%Na 1%%C4 H10 O3", "length": "125", "ligstr": "nan:A:Na 1:22.99:SODIUM ION:[Na+]:InChI=1S/Na/q+1:FKNQFGJONOIPTF-UHFFFAOYSA-N;GOL:B:C3 H8 O3:92.09:GLYCEROL:C(C(CO)O)O:InChI=1S/C3H8O3/c4-1-3(6)2-5/h3-6H,1-2H2:PEDCQBHIVMGVHV-UHFFFAOYSA-N;nan:B:Na 1:22.99:SODIUM ION:[Na+]:InChI=1S/Na/q+1:FKNQFGJONOIPTF-UHFFFAOYSA-N;PEG:B:C4 H10 O3:106.12:DI(HYDROXYETHYL)ETHER:C(COCCO)O:InChI=1S/C4H10O3/c5-1-3-7-4-2-6/h5-6H,1-4H2:MTHSVFCYNBDYFN-UHFFFAOYSA-N", "description": "They identify Beta-strands F and H as necessary for TTR aggregation. Based on the crystal structures of these segments, they designed two non-natural peptide inhibitors that block aggregation. This work provides the first characterization of peptide inhibitors for TTR aggregation, establishing a novel therapeutic strategy."}