{"global_stoichiometry": "Homo 4-mer - A4 ", "ligstr": "GOL:B:C3 H8 O3:92.09:GLYCEROL:C(C(CO)O)O:InChI=1S/C3H8O3/c4-1-3(6)2-5/h3-6H,1-2H2:PEDCQBHIVMGVHV-UHFFFAOYSA-N", "uniprot_ac": "P02766", "inchi": "InChI=1S/C3H8O3/c4-1-3(6)2-5/h3-6H,1-2H2", "reference": "J Biol Chem. 2015 Nov 27;290(48):28932-43.", "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.", "type": "Protein", "ligand_id": "GOL", "species": "Homo sapiens", "method": "X-RAY DIFFRACTION", "keyword": "Transthyretin", "gene_names": "TTR, PALB", "chain_id": "B", "ligand_mw": "92.09", "inchi_key": "PEDCQBHIVMGVHV-UHFFFAOYSA-N", "secondary_structure": "KCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTYAVVTNPKEHHHHHH#CCCEEEEEEETTTTEECTTCEEEEEEECTTSCEEEEEEEECCTTSEECCSCCTTTCCSEEEEEEECHHHHHHHTTCCCSEEEEEEEEEECCSSSCEEEEEEEEETTEEEEEEEEECCCCCCCCCC&KCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTYAVVTNPKEHHHHHH#CCCEEEEEEETTTTEECCSCEEEEEEECTTSCEEEEEEEECCTTSEECCSCCTTTCCSEEEEEEECHHHHHHHTTCCCSBSCEEEEEEESTTSCCEEEEEEEEETTEEEEEEEEECCCCCCCCCC", "amyloid_non_amyloid": "Amyloid", "length": "125", "remarks": "Crystal Structure of Human Transthyretin Thr119Tyr Mutant", "protein_name": "Transthyretin", "peptide_protein_sequence": "chain-ID A: KCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTYAVVTNPKEHHHHHH; chain-ID B: KCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTYAVVTNPKEHHHHHH", "ligand_name": "GLYCEROL", "ligand_smiles": "C(C(CO)O)O", "pdb_id": "4TNE", "ec_number": "", "pdb_classification": "TRANSPORT PROTEIN", "mutation_s_field": "T119Y", "ligand_formula": "C3 H8 O3", "r_value_free": "0.201", "alternative_name": "ATTR, Prealbumin, TBPA", "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.", "resolution": "1.55", "pmid": "26459562", "entry": "S-0396"}