{"method": "SOLUTION NMR", "mutation_s_field": "No", "ec_number": "", "description": "In patients afflicted with type 2 diabetes, amylin is found in fibrillar deposits in the pancreas. Membranes are thought to facilitate the aggregation of amylin, and membrane-bound oligomers may be responsible for the islet Beta-cell toxicity that develops during type 2 diabetes. The NMR structure of human amylin bound to SDS micelles was determined. The first four residues in the structure are constrained to form a hairpin loop by the single disulfide bond in amylin. The last nine residues near the C terminus are unfolded. The core of the structure is an Alpha-helix that runs from about residues 5-28. A distortion or kink near residues 18-22 introduces pliancy in the angle between the N- and C-terminal segments of the Alpha-helix.", "ligstr": "", "pmid": "19244249", "remarks": "The dynamic alpha-helix structure of micelle-bound human amylin", "amyloid_non_amyloid": "Amyloid", "type": "Peptide", "inchi": "", "resolution": "", "species": "Homo sapiens", "secondary_structure": "KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY#CCCSTTHHHHHHHHHHHHHHHHHHHHHTTSTTSCSCC", "chain_id": "", "gene_names": "IAPP", "r_value_free": "", "pdb_id": "2KB8", "reference": "J Biol Chem. 2009 May 1;284(18):11982-91.", "keyword": "Islet amyloid polypeptide", "protein_name": "Islet amyloid polypeptide", "ligand_formula": "", "peptide_protein_sequence": "chain-ID A: KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY", "entry": "S-0112", "length": "37", "uniprot_ac": "P10997", "author": "Patil, S.M., Xu, S., Sheftic, S.R., Alexandrescu, A.T.", "ligand_smiles": "", "ligand_mw": "", "alternative_name": "Amylin, Diabetes-associated peptide, Insulinoma amyloid peptide", "ligand_name": "", "pdb_classification": "HORMONE", "global_stoichiometry": "Monomer - A ", "inchi_key": "", "ligand_id": ""}