{"reference": "J Mol Biol. 2008 Oct 24;382(5):1157-67.", "alternative_name": "ATTR, Prealbumin, TBPA", "entry": "S-0207", "gene_names": "TTR, PALB", "remarks": "Crystal structure of human Transthyretin (TTR) at pH 4.0", "secondary_structure": "GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE#CCCCCCCCCCCEEEEEEETTTTEECTTCEEEEEEECTTSCEEEEEEEECCTTSEECCSCCTTTCCSEEEEEEECHHHHHHHTTCCCSEEEEEEEEEESTTSCCEEEEEEEEETTEEEEEEEEECCCC&GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE#CCCCCCCCCCCEEEEEEETTTTEECTTCEEEEEEECSSSCEEEEEEEECCTTSEECCSCCTTTCCSEEEEEEEECHHHHHHHTCCCCCCEEEEEEEESTTSCCEEEEEEEEETTEEEEEEEEECCCC", "chain_id": "", "inchi": "", "amyloid_non_amyloid": "Amyloid", "pmid": "18662699", "ligand_smiles": "", "keyword": "Transthyretin", "peptide_protein_sequence": "chain-ID A: GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE; chain-ID B: GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE", "uniprot_ac": "P02766", "protein_name": "Transthyretin", "r_value_free": "0.249", "mutation_s_field": "No", "ligand_mw": "", "pdb_id": "3D7P", "inchi_key": "", "ec_number": "", "pdb_classification": "TRANSPORT PROTEIN", "type": "Protein", "author": "Palaninathan, S.K., Mohamedmohaideen, N.N., Snee, W.C., Kelly, J.W., Sacchettini, J.C.", "species": "Homo sapiens", "ligand_id": "", "method": "X-RAY DIFFRACTION", "ligand_name": "", "global_stoichiometry": "Homo 4-mer - A4 ", "resolution": "1.72", "ligand_formula": "", "length": "127", "ligstr": "", "description": "To investigate the influence of acidification on the quaternary and tertiary structures of TTR, crystal structures of wild-type human TTR at pH 4.0 and pH 3.5 have been determined. In the pH 3.5 structure, the EF helix-loop region is completely disordered. These results demonstrate that acidic conditions increase the susceptibility of the EF helix-loop region of the TTR B subunit to undergo conformational changes and unfold, likely destabilizing the tetramer and identifying at least the initial conformational changes likely occurring within the tetramer that leads to the amyloidogenic monomer."}