| http://purl.uniprot.org/citations/16916844 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16916844 | http://www.w3.org/2000/01/rdf-schema#comment | "The crystal structure of the ternary complex of leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin (15-oxo-PG) 13-reductase (LTB4 12HD/PGR), an essential enzyme for eicosanoid inactivation pathways, with indomethacin and NADP+ has been solved. An indomethacin molecule bound in the anti-configuration at one of the two active site clefts of the homo-dimer interface in the LTB4 12HD/PGR and was confirmed by a binding calorimetry. The chlorobenzene ring is buried in the hydrophobic pore used as a binding site by the omega-chain of 15-oxo-PGE2. The carboxyl group interacts with the guanidino group of Arg56 and the phenolic hydroxyl group of Tyr262. Indomethacin shows a broad spectrum of efficacy against lipid-mediator related proteins including cyclooxygenase-2, phospholipase A2, PGF synthase and PGE synthase-2 but in the syn-configuration as well as LTB4 12HD/PGR in the anti-configuration. Indomethacin does not necessarily mimic the binding mode of the lipid-mediator substrates in the active sites of these complex structures. Thus, the broad spectrum of indomethacin efficacy can be attributed to its ability to adopt a range of different stable conformations. This allows the indomethacin to adapt to the distinct binding site features of each protein whilst maintaining favorable interactions between the carboxyl group and a counter charged functional group."xsd:string |
| http://purl.uniprot.org/citations/16916844 | http://purl.org/dc/terms/identifier | "doi:10.1093/jb/mvj176"xsd:string |
| http://purl.uniprot.org/citations/16916844 | http://purl.uniprot.org/core/author | "Ago H."xsd:string |
| http://purl.uniprot.org/citations/16916844 | http://purl.uniprot.org/core/author | "Miyano M."xsd:string |
| http://purl.uniprot.org/citations/16916844 | http://purl.uniprot.org/core/author | "Shimizu T."xsd:string |
| http://purl.uniprot.org/citations/16916844 | http://purl.uniprot.org/core/author | "Hori T."xsd:string |
| http://purl.uniprot.org/citations/16916844 | http://purl.uniprot.org/core/author | "Ishijima J."xsd:string |
| http://purl.uniprot.org/citations/16916844 | http://purl.uniprot.org/core/author | "Yokomizo T."xsd:string |
| http://purl.uniprot.org/citations/16916844 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16916844 | http://purl.uniprot.org/core/name | "J Biochem"xsd:string |
| http://purl.uniprot.org/citations/16916844 | http://purl.uniprot.org/core/pages | "457-466"xsd:string |
| http://purl.uniprot.org/citations/16916844 | http://purl.uniprot.org/core/title | "Crystal structure of anti-configuration of indomethacin and leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase complex reveals the structural basis of broad spectrum indomethacin efficacy."xsd:string |
| http://purl.uniprot.org/citations/16916844 | http://purl.uniprot.org/core/volume | "140"xsd:string |
| http://purl.uniprot.org/citations/16916844 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16916844 |
| http://purl.uniprot.org/citations/16916844 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16916844 |
| http://purl.uniprot.org/uniprot/#_Q9EQZ5-mappedCitation-16916844 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/16916844 |
| http://purl.uniprot.org/uniprot/Q9EQZ5 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/16916844 |