{"global_stoichiometry": "", "ligstr": "", "uniprot_ac": "P05067", "inchi": "", "reference": "J Biol Chem. 2006 Jan 27;281(4):2151-61. Epub  2005 Nov 21", "author": "Zirah, S., Kozin, S.A., Mazur, A.K., Blond, A., Cheminant, M., Segalas-Milazzo, I., Debey, P., Rebuffat, S.", "type": "Inhibitor complex", "ligand_id": "", "species": "Homo sapiens", "method": "SOLUTION NMR", "keyword": "AMYLOID BETA A4 PROTEIN", "gene_names": "", "chain_id": "", "ligand_mw": "", "inchi_key": "", "secondary_structure": "DAEFRHDSGYEVHHQK#CHHHHHHHHHHHHHCC", "amyloid_non_amyloid": "Non-amyloid", "length": "16", "remarks": "Zinc-binding domain of Alzheimer's disease amyloid beta-peptide in TFE-water (80-20) solution", "protein_name": "Amyloid-beta A4 protein", "peptide_protein_sequence": "chain-ID A: DAEFRHDSGYEVHHQK", "ligand_name": "", "ligand_smiles": "", "pdb_id": "2BP4", "ec_number": "", "pdb_classification": "AMYLOID PEPTIDE", "mutation_s_field": "No", "ligand_formula": "", "r_value_free": "", "alternative_name": "", "description": "the solution structure of the ABeta-(1-16)-Zn(2+) complex in aqueous solution at pH 6.5. The residues His(6), His(13), and His(14) and the Glu(11) carboxylate were identified as ligands that tetrahedrally coordinate the Zn(II) cation. In vitro aging experiments on ABeta-(1-16) led to the formation of truncated and isomerized species. The major isomer generated, ABeta-(1-16)-l-iso-Asp(7), displayed a local conformational change in the His(6)-Ser(8) region but kept a zinc binding propensity via a coordination mode involving l-iso-Asp(7). These results shows the potentiality of the region 1-16 of ABeta to be used as a therapeutic target. The absence of oligomerization upon zinc binding has also been shown.", "resolution": "", "pmid": "16301322", "entry": "S-0091"}