4EQU
Human STK-10 (LOK) kinase domain in DFG-out conformation with inhibitor DSA-7
Summary for 4EQU
| Entry DOI | 10.2210/pdb4equ/pdb |
| Descriptor | Serine/threonine-protein kinase 10, N-{3-[(3-{4-[(4-methoxyphenyl)amino]-1,3,5-triazin-2-yl}pyridin-2-yl)amino]-4-methylphenyl}-3-(trifluoromethyl)benzamide, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | serine/threonine kinase, transferase, transferase-transferase inhibitor complex, transferase/transferase inhibitor |
| Biological source | Homo sapiens (human) |
| Cellular location | Cell membrane; Peripheral membrane protein: O94804 |
| Total number of polymer chains | 2 |
| Total formula weight | 70178.98 |
| Authors | Merritt, E.A.,Larson, E.T. (deposition date: 2012-04-19, release date: 2012-11-07, Last modification date: 2024-11-27) |
| Primary citation | Ranjitkar, P.,Perera, B.G.,Swaney, D.L.,Hari, S.B.,Larson, E.T.,Krishnamurty, R.,Merritt, E.A.,Villen, J.,Maly, D.J. Affinity-Based Probes Based on Type II Kinase Inhibitors. J.Am.Chem.Soc., 134:19017-19025, 2012 Cited by PubMed Abstract: Protein kinases are key components of most mammalian signal transduction networks and are therapeutically relevant drug targets. Efforts to study protein kinase function would benefit from new technologies that are able to profile kinases in complex proteomes. Here, we describe active site-directed probes for profiling kinases in whole cell extracts and live cells. These probes contain general ligands that stabilize a specific inactive conformation of the ATP-binding sites of protein kinases, as well as trifluoromethylphenyl diazirine and alkyne moieties that allow covalent modification and enrichment of kinases, respectively. A diverse group of serine/threonine and tyrosine kinases were identified as specific targets of these probes in whole cell extracts. In addition, a number of kinase targets were selectively labeled in live cells. Our chemical proteomics approach should be valuable for interrogating protein kinase active sites in physiologically relevant environments. PubMed: 23088519DOI: 10.1021/ja306035v PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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