{"method": "SOLUTION NMR", "mutation_s_field": "No", "ec_number": "", "description": "The 3D structure of the fibrils comprising ABeta(1-42), which was obtained by using hydrogen-bonding constraints from quenched hydrogen/deuterium-exchange NMR, side-chain packing constraints from pairwise mutagenesis studies, and parallel, in-register Beta-sheet arrangement from previous solid-state NMR studies. Although residues 1-17 are disordered, residues 18-42 form a Beta-strand-turn-Beta-strand motif that contains two intermolecular, parallel, in-register Beta-sheets that are formed by residues 18-26 (Beta1) and 31-42 (Beta2). At least two molecules of ABeta(1-42) are required to achieve the repeating structure of a protofilament. Intermolecular side-chain contacts are formed between the odd-numbered residues of strand Beta1 of the nth molecule and the even-numbered residues of strand Beta2 of the (n - 1)th molecule. This interaction pattern leads to partially unpaired Beta-strands at the fibrillar ends, which explains the sequence selectivity, the cooperativity, and the apparent unidirectionality of ABeta fibril growth. It also provides a structural basis for fibrillization inhibitors.", "ligstr": "", "pmid": "16293696", "remarks": "3D Structure of Alzheimer's Abeta(1-42) fibrils", "amyloid_non_amyloid": "Amyloid", "type": "Fibril", "inchi": "", "resolution": "", "species": "Homo sapiens", "secondary_structure": "DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA#CCCCCCCCCCCCCCCCCEEEEEEEEESCCSEEEEEEEEEEEC&DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA#CCCCCCCCCCCCCCCCCEEEEEEEEESCCSEEEEEEEEEEEC&DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA#CCCCCCCCCCCCCCCCCEEEEEEEEESCCSEEEEEEEEEEEC&DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA#CCCCCCCCCCCCCCCCCEEEEEEEEESCCSEEEEEEEEEEEC&DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA#CCCCCCCCCCCCCCCCCEEEEEEEEESCCSEEEEEEEEEEEC", "chain_id": "", "gene_names": "APP, A4, AD1", "r_value_free": "", "pdb_id": "2BEG", "reference": "Proc Natl Acad Sci U S A. 2005 Nov 29;102(48):17342-7. Epub  2005 Nov 17", "keyword": "Amyloid beta A4 protein", "protein_name": "Amyloid-beta A4 protein", "ligand_formula": "", "peptide_protein_sequence": "chain-ID A: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA; chain-ID B: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA; chain-ID C: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA; chain-ID D: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA; chain-ID E: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA", "entry": "S-0089", "length": "42", "uniprot_ac": "P05067", "author": "Luhrs, T., Ritter, C., Adrian, M., Riek-Loher, D., Bohrmann, B., Dobeli, H., Schubert, D., Riek, R.", "ligand_smiles": "", "ligand_mw": "", "alternative_name": "ABPP, APPI, Alzheimer disease amyloid protein, Amyloid precursor protein, Amyloid-beta precursor protein, Cerebral vascular amyloid peptide, PreA4, Protease nexin-II", "ligand_name": "", "pdb_classification": "PROTEIN FIBRIL", "global_stoichiometry": "Homo 5-mer - A5", "inchi_key": "", "ligand_id": ""}