{"reference": "Protein Sci. 2018 Jul;27(7):1295-1303.", "alternative_name": "", "entry": "S-0511", "gene_names": "", "remarks": "AMYLOID FORMING PEPTIDE YTIAAL FROM TRANSTHYRETIN", "secondary_structure": "YTIAAL#CCCCCC", "chain_id": "", "inchi": "", "amyloid_non_amyloid": "Amyloid", "pmid": "29626847", "ligand_smiles": "", "keyword": "TYR-THR-ILE-ALA-ALA-LEU", "peptide_protein_sequence": "chain-ID A: YTIAAL", "uniprot_ac": "", "protein_name": "Transthyretin", "r_value_free": "0.244", "mutation_s_field": "No", "ligand_mw": "", "pdb_id": "6C3S", "inchi_key": "", "ec_number": "", "pdb_classification": "PROTEIN FIBRIL", "type": "Fibril", "author": "Saelices, L., Sievers, S.A., Sawaya, M.R., Eisenberg, D.S.", "species": "Homo sapiens", "ligand_id": "", "method": "X-RAY DIFFRACTION", "ligand_name": "", "global_stoichiometry": "Homo 20-mer - A20 ", "resolution": "1.6", "ligand_formula": "", "length": "6", "ligstr": "", "description": "They study amyloidogenic segments of transthyretin (TTR). TTR is a transporter of thyroxine and retinol in the blood and cerebrospinal fluid. When mutated and/or as a result of aging, TTR aggregates into amyloid fibrils that accumulate in organs such as the heart. The segments from the C-terminal region of TTR form in-register steric-zippers with highly-interdigitated, wet interfaces, whereas the Beta-strand B from the N-terminal region of TTR forms an out-of-register assembly, previously associated with oligomeric formation."}