| http://purl.uniprot.org/citations/1522586 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1522586 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1522586 | http://www.w3.org/2000/01/rdf-schema#comment | "The three-dimensional structure of human class pi glutathione S-transferase from placenta (hGSTP1-1), a homodimeric enzyme, has been solved by Patterson search methods and refined at 2.8 A resolution to a final crystallographic R-factor of 19.6% (8.0 to 2.8 A resolution). Subunit folding topology, subunit overall structure and subunit association closely resembles the structure of porcine class pi glutathione S-transferase. The binding site of a competitive inhibitor, S-hexylglutathione, is analyzed and the locations of the binding regions for glutathione (G-site) and electrophilic substrates (H-site) are determined. The specific interactions between protein and the inhibitor's glutathione peptide are the same as those observed between glutathione sulfonate and the porcine isozyme. The H-site is located adjacent to the G-site, with the hexyl moiety lying above a segment (residues 8 to 10) connecting strand beta 1 and helix alpha A where it is in hydrophobic contact with Tyr7, Phe8, Val10, Val35 and Tyr106. Catalytic models are discussed on the basis of the molecular structure."xsd:string |
| http://purl.uniprot.org/citations/1522586 | http://purl.org/dc/terms/identifier | "doi:10.1016/0022-2836(92)90692-d"xsd:string |
| http://purl.uniprot.org/citations/1522586 | http://purl.org/dc/terms/identifier | "doi:10.1016/0022-2836(92)90692-d"xsd:string |
| http://purl.uniprot.org/citations/1522586 | http://purl.uniprot.org/core/author | "Huber R."xsd:string |
| http://purl.uniprot.org/citations/1522586 | http://purl.uniprot.org/core/author | "Huber R."xsd:string |
| http://purl.uniprot.org/citations/1522586 | http://purl.uniprot.org/core/author | "Ladenstein R."xsd:string |
| http://purl.uniprot.org/citations/1522586 | http://purl.uniprot.org/core/author | "Ladenstein R."xsd:string |
| http://purl.uniprot.org/citations/1522586 | http://purl.uniprot.org/core/author | "Reinemer P."xsd:string |
| http://purl.uniprot.org/citations/1522586 | http://purl.uniprot.org/core/author | "Reinemer P."xsd:string |
| http://purl.uniprot.org/citations/1522586 | http://purl.uniprot.org/core/author | "Parker M.W."xsd:string |
| http://purl.uniprot.org/citations/1522586 | http://purl.uniprot.org/core/author | "Parker M.W."xsd:string |
| http://purl.uniprot.org/citations/1522586 | http://purl.uniprot.org/core/author | "Federici G."xsd:string |
| http://purl.uniprot.org/citations/1522586 | http://purl.uniprot.org/core/author | "Federici G."xsd:string |
| http://purl.uniprot.org/citations/1522586 | http://purl.uniprot.org/core/author | "Lo Bello M."xsd:string |
| http://purl.uniprot.org/citations/1522586 | http://purl.uniprot.org/core/author | "Lo Bello M."xsd:string |
| http://purl.uniprot.org/citations/1522586 | http://purl.uniprot.org/core/author | "Dirr H.W."xsd:string |
| http://purl.uniprot.org/citations/1522586 | http://purl.uniprot.org/core/author | "Dirr H.W."xsd:string |
| http://purl.uniprot.org/citations/1522586 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
| http://purl.uniprot.org/citations/1522586 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
| http://purl.uniprot.org/citations/1522586 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
| http://purl.uniprot.org/citations/1522586 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
| http://purl.uniprot.org/citations/1522586 | http://purl.uniprot.org/core/pages | "214-226"xsd:string |
| http://purl.uniprot.org/citations/1522586 | http://purl.uniprot.org/core/pages | "214-226"xsd:string |