| http://purl.uniprot.org/citations/23431194 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23431194 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23431194 | http://www.w3.org/2000/01/rdf-schema#comment | "Prostaglandin E2 (PGE2) is a key mediator in inflammatory response. The main source of inducible PGE2, microsomal PGE2 synthase-1 (mPGES-1), has emerged as an interesting drug target for treatment of pain. To support inhibitor design, we have determined the crystal structure of human mPGES-1 to 1.2 Å resolution. The structure reveals three well-defined active site cavities within the membrane-spanning region in each monomer interface of the trimeric structure. An important determinant of the active site cavity is a small cytosolic domain inserted between transmembrane helices I and II. This extra domain is not observed in other structures of proteins within the MAPEG (Membrane-Associated Proteins involved in Eicosanoid and Glutathione metabolism) superfamily but is likely to be present also in microsomal GST-1 based on sequence similarity. An unexpected feature of the structure is a 16-Å-deep cone-shaped cavity extending from the cytosolic side into the membrane-spanning region. We suggest a potential role for this cavity in substrate access. Based on the structure of the active site, we propose a catalytic mechanism in which serine 127 plays a key role. We have also determined the structure of mPGES-1 in complex with a glutathione-based analog, providing insight into mPGES-1 flexibility and potential for structure-based drug design."xsd:string |
| http://purl.uniprot.org/citations/23431194 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.1218504110"xsd:string |
| http://purl.uniprot.org/citations/23431194 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.1218504110"xsd:string |
| http://purl.uniprot.org/citations/23431194 | http://purl.uniprot.org/core/author | "Liu G."xsd:string |
| http://purl.uniprot.org/citations/23431194 | http://purl.uniprot.org/core/author | "Liu G."xsd:string |
| http://purl.uniprot.org/citations/23431194 | http://purl.uniprot.org/core/author | "Johansson P."xsd:string |
| http://purl.uniprot.org/citations/23431194 | http://purl.uniprot.org/core/author | "Johansson P."xsd:string |
| http://purl.uniprot.org/citations/23431194 | http://purl.uniprot.org/core/author | "Nord J."xsd:string |
| http://purl.uniprot.org/citations/23431194 | http://purl.uniprot.org/core/author | "Nord J."xsd:string |
| http://purl.uniprot.org/citations/23431194 | http://purl.uniprot.org/core/author | "Geschwindner S."xsd:string |
| http://purl.uniprot.org/citations/23431194 | http://purl.uniprot.org/core/author | "Geschwindner S."xsd:string |
| http://purl.uniprot.org/citations/23431194 | http://purl.uniprot.org/core/author | "Sjogren T."xsd:string |
| http://purl.uniprot.org/citations/23431194 | http://purl.uniprot.org/core/author | "Sjogren T."xsd:string |
| http://purl.uniprot.org/citations/23431194 | http://purl.uniprot.org/core/author | "Ek M."xsd:string |
| http://purl.uniprot.org/citations/23431194 | http://purl.uniprot.org/core/author | "Ek M."xsd:string |
| http://purl.uniprot.org/citations/23431194 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23431194 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23431194 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/23431194 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/23431194 | http://purl.uniprot.org/core/pages | "3806-3811"xsd:string |
| http://purl.uniprot.org/citations/23431194 | http://purl.uniprot.org/core/pages | "3806-3811"xsd:string |
| http://purl.uniprot.org/citations/23431194 | http://purl.uniprot.org/core/title | "Crystal structure of microsomal prostaglandin E2 synthase provides insight into diversity in the MAPEG superfamily."xsd:string |
| http://purl.uniprot.org/citations/23431194 | http://purl.uniprot.org/core/title | "Crystal structure of microsomal prostaglandin E2 synthase provides insight into diversity in the MAPEG superfamily."xsd:string |