{"reference": "Proc Natl Acad Sci U S A. 2014 Jan 28;111(4):1539-44.", "alternative_name": "ATTR, Prealbumin, TBPA", "entry": "S-0342", "gene_names": "TTR, PALB", "remarks": "Human Transthyretin Ser52Pro Mutant", "secondary_structure": "PTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSEPGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE#CCCCCCCCCCEEEEEEETTTTEECCSCEEEEEEECTTSCEEEEEEEECCTTSEECCSCCTTTCCSEEEEEEECHHHHHHHTTCCCSEEEEEEEEEESTTSCCEEEEEEEEETTEEEEEEEEECCCC&PTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSEPGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE#CCCCCCCCCCEEEEEEETTTTEECCSCEEEEEEECTTSCEEEEEEEECCTTSEECCSCCTTTCCSEEEEEEECHHHHHHHTTCCCSEEEEEEEEEECCCCCCEEEEEEEEETTEEEEEEEEECCCC", "chain_id": "A%%B", "inchi": "InChI=1S/Ca/q+2%%InChI=1S/Ca/q+2", "amyloid_non_amyloid": "Amyloid", "pmid": "24474780", "ligand_smiles": "[Ca+2]%%[Ca+2]", "keyword": "Transthyretin", "peptide_protein_sequence": "chain-ID A: PTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSEPGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE; chain-ID B: PTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSEPGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE", "uniprot_ac": "P02766", "protein_name": "Transthyretin", "r_value_free": "0.228", "mutation_s_field": "S52P", "ligand_mw": "40.08%%40.08", "pdb_id": "4MRC", "inchi_key": "BHPQYMZQTOCNFJ-UHFFFAOYSA-N%%BHPQYMZQTOCNFJ-UHFFFAOYSA-N", "ec_number": "", "pdb_classification": "TRANSPORT PROTEIN", "type": "Protein", "author": "Mangione, P.P., Porcari, R., Gillmore, J.D., Pucci, P., Monti, M., Porcari, M., Giorgetti, S., Marchese, L., Raimondi, S., Serpell, L.C., Chen, W., Relini, A., Marcoux, J., Clatworthy, I.R., Taylor, G.W., Tennent, G.A., Robinson, C.V., Hawkins, P.N., Stop", "species": "Homo sapiens", "ligand_id": "CA%%CA", "method": "X-RAY DIFFRACTION", "ligand_name": "CALCIUM ION%%CALCIUM ION", "global_stoichiometry": "Homo 4-mer - A4 ", "resolution": "1.54", "ligand_formula": "Ca 2%%Ca 2", "length": "126", "ligstr": "CA:A:Ca 2:40.08:CALCIUM ION:[Ca+2]:InChI=1S/Ca/q+2:BHPQYMZQTOCNFJ-UHFFFAOYSA-N;CA:B:Ca 2:40.08:CALCIUM ION:[Ca+2]:InChI=1S/Ca/q+2:BHPQYMZQTOCNFJ-UHFFFAOYSA-N", "description": "The Ser52Pro variant of transthyretin (TTR) produces aggressive, highly penetrant, autosomal-dominant systemic amyloidosis in persons heterozygous for the causative mutation. Wild-type TTR and other TTR variants has been reported to be the principal constituent of type A, cardiac amyloid fibrils formed. In physiological conditions and under agitation the residue 49-127 proteolytic fragment rapidly and completely self-aggregates into typical amyloid fibrils. The remarkable susceptibility to such cleavage is likely caused by localized destabilization of the Beta-turn linking strands C and D caused by loss of the wild-type hydrogen-bonding network between the side chains of residues Ser52, Glu54, Ser50, and a water molecule."}