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• W1990454181 endingPage "466" @default.
• W1990454181 startingPage "457" @default.
• W1990454181 abstract "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 ω-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." @default.
• W1990454181 created "2016-06-24" @default.
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• W1990454181 date "2006-09-01" @default.
• W1990454181 modified "2023-09-26" @default.
• W1990454181 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" @default.
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• W1990454181 doi "https://doi.org/10.1093/jb/mvj176" @default.
• W1990454181 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16916844" @default.
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