{"reference": "J Biol Chem. 2015 Nov 27;290(48):28932-43.", "alternative_name": "", "entry": "S-0406", "gene_names": "", "remarks": "Structure of an amyloid-forming segment TAVVTN from human Transthyretin", "secondary_structure": "TAVVTN#CCCCCC", "chain_id": "", "inchi": "", "amyloid_non_amyloid": "Amyloid", "pmid": "26459562", "ligand_smiles": "", "keyword": "Amyloid-forming peptide TAVVTN", "peptide_protein_sequence": "chain-ID A: TAVVTN", "uniprot_ac": "", "protein_name": "Transthyretin", "r_value_free": "0.14800000", "mutation_s_field": "No", "ligand_mw": "", "pdb_id": "4XFO", "inchi_key": "", "ec_number": "", "pdb_classification": "PROTEIN FIBRIL", "type": "Fibril", "author": "Saelices, L., Johnson, L.M., Liang, W.Y., Sawaya, M.R., Cascio, D., Ruchala, P., Whitelegge, J., Jiang, L., Riek, R., Eisenberg, D.S.", "species": "synthetic construct", "ligand_id": "", "method": "X-RAY DIFFRACTION", "ligand_name": "", "global_stoichiometry": "", "resolution": "1.35", "ligand_formula": "", "length": "6", "ligstr": "", "description": "They identify Beta-strands F and H as necessary for TTR aggregation. Based on the crystal structures of these segments, they designed two non-natural peptide inhibitors that block aggregation. This work provides the first characterization of peptide inhibitors for TTR aggregation, establishing a novel therapeutic strategy."}