4WNP
Structure of ULK1 bound to a potent inhibitor
Summary for 4WNP
| Entry DOI | 10.2210/pdb4wnp/pdb |
| Related | 4WNO |
| Descriptor | Serine/threonine-protein kinase ULK1, GLYCEROL, N~2~-(1H-benzimidazol-6-yl)-N~4~-(5-cyclobutyl-1H-pyrazol-3-yl)quinazoline-2,4-diamine, ... (4 entities in total) |
| Functional Keywords | kinase, autophagy, inhibitor, transferase-transferase inhibitor complex, transferase/transferase inhibitor |
| Biological source | Homo sapiens (Human) |
| Cellular location | Cytoplasm, cytosol : O75385 |
| Total number of polymer chains | 4 |
| Total formula weight | 131051.03 |
| Authors | Lazarus, M.B.,Novotny, C.J.,Shokat, K.M. (deposition date: 2014-10-14, release date: 2015-01-14, Last modification date: 2024-11-13) |
| Primary citation | Lazarus, M.B.,Novotny, C.J.,Shokat, K.M. Structure of the Human Autophagy Initiating Kinase ULK1 in Complex with Potent Inhibitors. Acs Chem.Biol., 10:257-261, 2015 Cited by PubMed Abstract: Autophagy is a conserved cellular process that involves the degradation of cellular components for energy maintenance and cytoplasmic quality control that has recently gained interest as a novel target for a variety of human diseases, including cancer. A prime candidate to determine the potential therapeutic benefit of targeting autophagy is the kinase ULK1, whose activation initiates autophagy. Here, we report the first structures of ULK1, in complex with multiple potent inhibitors. These structures show features unique to the enzyme and will provide a path for the rational design of selective compounds as cellular probes and potential therapeutics. PubMed: 25551253DOI: 10.1021/cb500835z PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.88 Å) |
Structure validation
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