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Crystal Structure of P38 Kinase in Complex with A Biaryl Amide InhibitorCrystal Structure of P38 Kinase in Complex with A Biaryl Amide 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 PubMedNew kinase inhibitors can be found by synthesis of targeted arrays of compounds designed using system-based knowledge as well as through screening focused or diverse compounds. Most array strategies aim to add functionality to a fragment that binds in the purine subpocket of the ATP-site. Here, an alternative pharmacophore-guided array approach is described which set out to discover novel purine subpocket-binding groups. Results are shown for p38alpha and cFMS kinase, for which multiple distinct series with nanomolar potency were discovered. Some of the compounds showed potency in cell-based assays and good pharmacokinetic properties. Kinase array design, back to front: biaryl amides.,Baldwin I, Bamborough P, Haslam CG, Hunjan SS, Longstaff T, Mooney CJ, Patel S, Quinn J, Somers DO Bioorg Med Chem Lett. 2008 Oct 1;18(19):5285-9. Epub 2008 Aug 22. PMID:18789685[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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