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Crystal structure of human PIM-1 Kinase in complex with inhibitorCrystal structure of human PIM-1 Kinase in complex with inhibitor
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedA novel series of highly potent substituted pyridone Pim-1 kinase inhibitors is described. Structural requirements for in vitro activity are outlined as well as a complex crystal structure with the most potent Pim-1 inhibitor reported (IC(50)=50 nM). A hydrogen bond matrix involving the Pim-1 inhibitor, two water molecules, and the catalytic core, together with a potential weak hydrogen bond between an aromatic hydrogen on the R(1) phenyl ring and a main-chain carbonyl of Pim-1, accounts for the overall potency of this inhibitor. Identification and structure-activity relationships of substituted pyridones as inhibitors of Pim-1 kinase.,Cheney IW, Yan S, Appleby T, Walker H, Vo T, Yao N, Hamatake R, Hong Z, Wu JZ Bioorg Med Chem Lett. 2007 Mar 15;17(6):1679-83. Epub 2007 Jan 4. PMID:17251021[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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