{"resolution": "", "ligand_mw": "", "secondary_structure": "DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA#CCSSSTTHHHHHHHHHHHHHHHHHHTTHHHHHHHHHHHHSCC", "inchi": "", "method": "SOLUTION NMR", "ec_number": "", "uniprot_ac": "P05067", "remarks": "Solution structure of the Alzheimer's disease amyloid beta-peptide (1-42)", "description": "Exhaustive solvent scan performed showed a high propensity of ABeta-(1-42) to adopt helical conformations in aqueous solutions of fluorinated alcohols. The 3D NMR structure of ABeta-(1-42) shows two helical regions encompassing residues 8-25 and 28-38, connected by a regular type I Beta-turn. The surprising similarity of this structure, as well as the sequence of the C-terminal moiety, with those of the fusion domain of influenza hemagglutinin suggests a direct mechanism of neurotoxicity.", "type": "Peptide", "ligand_smiles": "", "chain_id": "", "species": "Homo sapiens", "keyword": "Alzheimer's disease amyloid", "ligstr": "", "pmid": "12423364", "mutation_s_field": "No", "author": "Crescenzi, O., Tomaselli, S., Guerrini, R., Salvadori, S., D'Ursi, A.M., Temussi, P.A., Picone, D.", "pdb_id": "1IYT", "amyloid_non_amyloid": "Amyloid", "inchi_key": "", "ligand_name": "", "ligand_formula": "", "ligand_id": "", "r_value_free": "", "protein_name": "Amyloid-beta A4 protein", "gene_names": "APP, A4, AD1", "global_stoichiometry": "Monomer - A", "alternative_name": "ABPP, APPI, Alzheimer disease amyloid protein, Amyloid precursor protein, Amyloid-beta precursor protein, Cerebral vascular amyloid peptide, PreA4, Protease nexin-II", "peptide_protein_sequence": "chain-ID A: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA", "pdb_classification": "PROTEIN BINDING", "reference": "Eur J Biochem. 2002 Nov;269(22):5642-8", "length": "42", "entry": "S-0037"}