{"reference": "Sci Rep. 2017 Mar 13;7:44041.", "alternative_name": "Amylin, Diabetes-associated peptide, Insulinoma amyloid peptide", "entry": "S-0447", "gene_names": "IAPP", "remarks": "Solution structure of oxidized and amidated human IAPP (1-37), the diabetes II peptide.", "secondary_structure": "KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTX#CCCSTTTHHHHHHHHSSSCTTTTTTTSSSTTSSSCCC", "chain_id": "A", "inchi": "InChI=1S/C9H12N2O2/c10-8(9(11)13)5-6-1-3-7(12)4-2-6/h1-4,8,12H,5,10H2,(H2,11,13)/t8-/m0/s1", "amyloid_non_amyloid": "Amyloid", "pmid": "28287098", "ligand_smiles": "c1cc(ccc1C[C@@H](C(=O)N)N)O", "keyword": "Islet amyloid polypeptide", "peptide_protein_sequence": "chain-ID A: KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTX", "uniprot_ac": "P10997", "protein_name": "Islet amyloid polypeptide", "r_value_free": "", "mutation_s_field": "No", "ligand_mw": "180.2", "pdb_id": "5MGQ", "inchi_key": "PQFMNVGMJJMLAE-QMMMGPOBSA-N", "ec_number": "", "pdb_classification": "PROTEIN FIBRIL", "type": "Peptide", "author": "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,", "species": "Homo sapiens", "ligand_id": "TYC", "method": "SOLUTION NMR", "ligand_name": "L-TYROSINAMIDE", "global_stoichiometry": "Monomer - A", "resolution": "", "ligand_formula": "C9 H12 N2 O2", "length": "37", "ligstr": "TYC:A:C9 H12 N2 O2:180.2:L-TYROSINAMIDE:c1cc(ccc1C[C@@H](C(=O)N)N)O:InChI=1S/C9H12N2O2/c10-8(9(11)13)5-6-1-3-7(12)4-2-6/h1-4,8,12H,5,10H2,(H2,11,13)/t8-/m0/s1:PQFMNVGMJJMLAE-QMMMGPOBSA-N", "description": "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."}