{"global_stoichiometry": "Homo 4-mer - A4 ", "ligstr": "DIU:A:C7 H4 I2 O3:389.91:2-HYDROXY-3,5-DIIODO-BENZOIC ACID:c1c(cc(c(c1C(=O)O)O)I)I:InChI=1S/C7H4I2O3/c8-3-1-4(7(11)12)6(10)5(9)2-3/h1-2,10H,(H,11,12):DHZVWQPHNWDCFS-UHFFFAOYSA-N;DIU:B:C7 H4 I2 O3:389.91:2-HYDROXY-3,5-DIIODO-BENZOIC ACID:c1c(cc(c(c1C(=O)O)O)I)I:InChI=1S/C7H4I2O3/c8-3-1-4(7(11)12)6(10)5(9)2-3/h1-2,10H,(H,11,12):DHZVWQPHNWDCFS-UHFFFAOYSA-N", "uniprot_ac": "P02766", "inchi": "InChI=1S/C7H4I2O3/c8-3-1-4(7(11)12)6(10)5(9)2-3/h1-2,10H,(H,11,12)%%InChI=1S/C7H4I2O3/c8-3-1-4(7(11)12)6(10)5(9)2-3/h1-2,10H,(H,11,12)", "reference": "Biochim Biophys Acta. 2008 Mar;1784(3):512-7. Epub  2007 Dec 3", "author": "Gales, L., Almeida, M.R., Arsequell, G., Valencia, G., Saraiva, M.J., Damas, A.M.", "type": "Inhibitor complex", "ligand_id": "DIU%%DIU", "species": "Homo sapiens", "method": "X-RAY DIFFRACTION", "keyword": "Transthyretin", "gene_names": "TTR, PALB", "chain_id": "A%%B", "ligand_mw": "389.91%%389.91", "inchi_key": "DHZVWQPHNWDCFS-UHFFFAOYSA-N%%DHZVWQPHNWDCFS-UHFFFAOYSA-N", "secondary_structure": "GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE#CCCCCCCCCCCEEEEEEETTTTEECTTCEEEEEEECTTSSEEEEEEEECCTTSEECCSCCTTTCCSEEEEEEECHHHHHHHTTCCCSEEEEEEEEEESTTSCCEEEEEEEEETTEEEEEEEEECCCC&GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE#CCCCCCCCCCCEEEEEEETTTTEECTTCEEEEEEECTTSCEEEEEEEECCTTSEECCSCCTTTCCSEEEEEEECHHHHHHHTTCCCSEEEEEEEEEECCSSSCEEEEEEEEETTEEEEEEEEECCCC", "amyloid_non_amyloid": "Non-amyloid", "length": "127", "remarks": "Crystal structure of transthyretin in complex with 3,5-diiodosalicylic acid", "protein_name": "Transthyretin", "peptide_protein_sequence": "chain-ID A: GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE; chain-ID B: GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE", "ligand_name": "2-HYDROXY-3,5-DIIODO-BENZOIC ACID%%2-HYDROXY-3,5-DIIODO-BENZOIC ACID", "ligand_smiles": "c1c(cc(c(c1C(=O)O)O)I)I%%c1c(cc(c(c1C(=O)O)O)I)I", "pdb_id": "3B56", "ec_number": "", "pdb_classification": "TRANSPORT PROTEIN", "mutation_s_field": "No", "ligand_formula": "C7 H4 I2 O3%%C7 H4 I2 O3", "r_value_free": "0.214", "alternative_name": "ATTR, Prealbumin, TBPA", "description": "A number of structurally diverse small molecules that bind to the TTR channel increasing the protein stability and thereafter inhibiting amyloid fibrillogenesis have been tested. In order to take advantage of the high propensity to interactions between iodine substituents and the TTR channel. they have identified iodinated derivative of salicylic acid 3,5-diiodosalicylic acid, available commercially. The paper reports relative binding affinities of salicylic acid and the iodinated derivative and the crystal structure of TTR complexed with 3,5-diiodosalicylic acid, to elucidate the higher binding affinity of this compound towards TTR.", "resolution": "1.55", "pmid": "18155178", "entry": "S-0187"}