{"global_stoichiometry": "Homo 4-mer - A4 ", "ligstr": "", "uniprot_ac": "P02766", "inchi": "", "reference": "J Mol Biol. 2007 Feb 23;366(3):711-9. Epub  2006 Dec 1", "author": "Pasquato, N., Berni, R., Folli, C., Alfieri, B., Cendron, L., Zanotti, G.", "type": "Protein", "ligand_id": "", "species": "Homo sapiens", "method": "X-RAY DIFFRACTION", "keyword": "Transthyretin", "gene_names": "TTR, PALB", "chain_id": "", "ligand_mw": "", "inchi_key": "", "secondary_structure": "GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE#CCCCCCCCCCCEEEEEEETTTTEECTTCEEEEEEECTTSCEEEEEEEECCTTSEECCSCCTTTCCSEEEEEEECHHHHHHHTTCCCSEEEEEEEEEESTTSCCEEEEEEEEETTEEEEEEEEECCCC&GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE#CCCCCCCCCCCEEEEEEETTTTEECTTCEEEEEEECTTSCEEEEEEEECCTTSEECCSCCTTTCCSEEEEEEECHHHHHHHTTCCCSEEEEEEEEEECTTSCSEEEEEEEEETTEEEEEEEEECCCC", "amyloid_non_amyloid": "Amyloid", "length": "127", "remarks": "Crystal structure of human transthyretin at pH 4.6", "protein_name": "Transthyretin", "peptide_protein_sequence": "chain-ID A: GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE; chain-ID B: GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE", "ligand_name": "", "ligand_smiles": "", "pdb_id": "2G4G", "ec_number": "", "pdb_classification": "TRANSPORT PROTEIN", "mutation_s_field": "No", "ligand_formula": "", "r_value_free": "0.233", "alternative_name": "ATTR, Prealbumin, TBPA", "description": "In vitro, the natural amyloidogenic I84S and the non-natural I84A TTR mutant forms exhibit a propensity to produce fibrils in an acidic medium significantly higher than that of wild-type TTR. The two mutant forms have been crystallized at both neutral and acidic pH. Their neutral pH crystal structures are very similar to that of wild-type TTR, consistent with previous evidence indicating that only minor structural changes are induced by amyloidogenic mutations. On the contrary, their crystal structures at moderately low pH (4.6) show significant conformational differences as compared to their neutral pH structures. Remarkably, such changes are not induced in wild-type TTR crystallized at low pH. The most relevant consist of the unwinding of the TTR short Alpha-helix and of the change in conformation of the loop connecting the Alpha-helix to Beta-strand F. Only one monomer of the crystallographic dimer is affected, causing a disruption of the tetrameric symmetry. This asymmetry and a possible destabilization of the tetrameric quaternary structure of TTR may be responsible for the amyloidogenic potential of the two TTR mutant forms at low pH.", "resolution": "1.85", "pmid": "17196219", "entry": "S-0106"}