5CI7
Structure of ULK1 bound to a selective inhibitor
Summary for 5CI7
| Entry DOI | 10.2210/pdb5ci7/pdb |
| Related | 4WNO |
| Descriptor | Serine/threonine-protein kinase ULK1, N-[3-({4-[(3-aminopropyl)amino]-5-iodopyrimidin-2-yl}amino)phenyl]pyrrolidine-1-carboxamide, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | inhibitor, kinase, autophagy, transferase-transferase inhibitor complex, transferase/transferase inhibitor |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 33077.88 |
| Authors | Lazarus, M.B.,Shokat, K.M. (deposition date: 2015-07-11, release date: 2015-08-26, Last modification date: 2023-09-27) |
| Primary citation | Lazarus, M.B.,Shokat, K.M. Discovery and structure of a new inhibitor scaffold of the autophagy initiating kinase ULK1. Bioorg.Med.Chem., 23:5483-5488, 2015 Cited by PubMed Abstract: Energy homeostasis in eukaryotic cells is a complex and fundamental process that is misregulated in several human diseases. A key component of energy regulation is a process called autophagy that involves the recycling of cellular components. There has been much recent interest in studying the mechanism of autophagy to understand an important cellular process and to evaluate the therapeutic potential in targeting autophagy. Activation of a kinase called ULK1 initiates autophagy by driving downstream pathways that lead to the formation of double membrane bound vesicles that surround the cellular contents that are to be degraded. Here, we report the discovery of an inhibitor of ULK1 with improved selectivity and a high-resolution crystal structure of the compound bound to the kinase, which will be useful tools for studying autophagy in cells. PubMed: 26275681DOI: 10.1016/j.bmc.2015.07.034 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.74 Å) |
Structure validation
Download full validation report
