3E93
Crystal Structure of P38 Kinase in Complex with A Biaryl Amide Inhibitor
Summary for 3E93
| Entry DOI | 10.2210/pdb3e93/pdb |
| Related | 3E92 |
| Descriptor | Mitogen-activated protein kinase 14, 4-methyl-N-(3-morpholin-4-ylphenyl)-3-(3-piperidin-4-yl-1,2-benzisoxazol-6-yl)benzamide, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | p38, serine/threonine protein kinase, map kinase, atp-binding, kinase, nucleotide-binding, nucleus, phosphoprotein, serine/threonine-protein kinase, transferase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm : Q16539 |
| Total number of polymer chains | 1 |
| Total formula weight | 43439.62 |
| Authors | Somers, D.O.,Patel, S. (deposition date: 2008-08-21, release date: 2008-09-30, Last modification date: 2024-10-16) |
| Primary citation | Baldwin, I.,Bamborough, P.,Haslam, C.G.,Hunjan, S.S.,Longstaff, T.,Mooney, C.J.,Patel, S.,Quinn, J.,Somers, D.O. Kinase array design, back to front: Biaryl amides Bioorg.Med.Chem.Lett., 18:5285-5289, 2008 Cited by PubMed Abstract: New 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. PubMed: 18789685DOI: 10.1016/j.bmcl.2008.08.051 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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