{"resolution": "1.7", "ligand_mw": "286.24%%22.99%%286.24", "secondary_structure": "GPTGTGESKCPLMVKVLDAVRGSPAINVAMHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE#CCCCCCCCCCCEEEEEEETTTTEECTTCEEEEEEECTTSCEEEEEEEECCTTSEECCSCCTTTCCSEEEEEEECHHHHHHHTTCCCSEEEEEEEEEESTTSCCEEEEEEEEETTEEEEEEEEECCCC&GPTGTGESKCPLMVKVLDAVRGSPAINVAMHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE#CCCCCCCCCCCEEEEEEETTTTEECTTCEEEEEEECTTSCEEEEEEEECCTTSEECCSCCTTTCCSEEEEEEECHHHHHHHTTCCCSEEEEEEEEEECTTSCSEEEEEEEEETTEEEEEEEEECCCC", "inchi": "InChI=1S/C15H10O6/c16-8-4-11(19)15-12(20)6-13(21-14(15)5-8)7-1-2-9(17)10(18)3-7/h1-6,16-19H%%InChI=1S/Na/q+1%%InChI=1S/C15H10O6/c16-8-4-11(19)15-12(20)6-13(21-14(15)5-8)7-1-2-9(17)10(18)3-7/h1-6,16-19H", "method": "X-RAY DIFFRACTION", "ec_number": "", "uniprot_ac": "P02766", "remarks": "Crystal structure of human transthyretin variant V30M in complex with luteolin", "description": "They generated high-resolution crystal-structures of both TTR wild type and the amyloidogenic mutant V30M in complex with luteolin. The results show that the A-ring of luteolin, in contrast to what was previously suggested, is buried within the TBS, consequently explaining the lack of activity from cynaroside. The flavonoids represent an interesting group of drug candidates for TTR amyloidosis. The present investigation shows the potential of luteolin as a stabilizer of TTR in vivo.", "type": "Inhibitor complex", "ligand_smiles": "c1cc(c(cc1C2=CC(=O)c3c(cc(cc3O2)O)O)O)O%%[Na+]%%c1cc(c(cc1C2=CC(=O)c3c(cc(cc3O2)O)O)O)O", "chain_id": "A%%A%%B", "species": "Homo sapiens", "keyword": "Transthyretin", "ligstr": "LU2:A:C15 H10 O6:286.24:2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-4H-chromen-4-one:c1cc(c(cc1C2=CC(=O)c3c(cc(cc3O2)O)O)O)O:InChI=1S/C15H10O6/c16-8-4-11(19)15-12(20)6-13(21-14(15)5-8)7-1-2-9(17)10(18)3-7/h1-6,16-19H:IQPNAANSBPBGFQ-UHFFFAOYSA-N;nan:A:Na 1:22.99:SODIUM ION:[Na+]:InChI=1S/Na/q+1:FKNQFGJONOIPTF-UHFFFAOYSA-N;LU2:B:C15 H10 O6:286.24:2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-4H-chromen-4-one:c1cc(c(cc1C2=CC(=O)c3c(cc(cc3O2)O)O)O)O:InChI=1S/C15H10O6/c16-8-4-11(19)15-12(20)6-13(21-14(15)5-8)7-1-2-9(17)10(18)3-7/h1-6,16-19H:IQPNAANSBPBGFQ-UHFFFAOYSA-N", "pmid": "26020516", "mutation_s_field": "V30M ", "author": "Iakovleva, I., Begum, A., Pokrzywa, M., Walfridsson, M., Sauer-Eriksson, A.E., Olofsson, A.", "pdb_id": "4QYA", "amyloid_non_amyloid": "Non-amyloid", "inchi_key": "IQPNAANSBPBGFQ-UHFFFAOYSA-N%%FKNQFGJONOIPTF-UHFFFAOYSA-N%%IQPNAANSBPBGFQ-UHFFFAOYSA-N", "ligand_name": "2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-4H-chromen-4-one%%SODIUM ION%%2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-4H-chromen-4-one", "ligand_formula": "C15 H10 O6%%Na 1%%C15 H10 O6", "ligand_id": "LU2%%nan%%LU2", "r_value_free": "0.198", "protein_name": "Transthyretin", "gene_names": "TTR, PALB", "global_stoichiometry": "Homo 4-mer - A4 ", "alternative_name": "ATTR, Prealbumin, TBPA", "peptide_protein_sequence": "chain-ID A: GPTGTGESKCPLMVKVLDAVRGSPAINVAMHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE; chain-ID B: GPTGTGESKCPLMVKVLDAVRGSPAINVAMHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE", "pdb_classification": "TRANSPORT PROTEIN", "reference": "PLoS One. 2015 May 28;10(5):e0128222.", "length": "127", "entry": "S-0375"}