8ANS
Crystal structure of D1228V c-MET bound by compound 1.
Summary for 8ANS
| Entry DOI | 10.2210/pdb8ans/pdb |
| Descriptor | Hepatocyte growth factor receptor, GLYCEROL, 3-[bis(fluoranyl)methyl]-~{N}-methyl-~{N}-[(1~{R})-8-methyl-5-(3-methyl-1~{H}-indazol-6-yl)-1,2,3,4-tetrahydronaphthalen-1-yl]pyridine-2-carboxamide, ... (4 entities in total) |
| Functional Keywords | kinase, inhibitor, ac-helix, cancer, transferase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 34008.52 |
| Authors | Collie, G.W. (deposition date: 2022-08-05, release date: 2022-08-31, Last modification date: 2024-01-31) |
| Primary citation | Collie, G.W.,Barlind, L.,Bazzaz, S.,Borjesson, U.,Dale, I.L.,Disch, J.S.,Habeshian, S.,Jetson, R.,Khurana, P.,Madin, A.,Michaelides, I.N.,Peng, L.,Snijder, A.,Stubbs, C.J. Discovery of a selective c-MET inhibitor with a novel binding mode. Bioorg.Med.Chem.Lett., 75:128948-128948, 2022 Cited by PubMed Abstract: The c-MET receptor tyrosine kinase has received considerable attention as a cancer drug target yet there remains a need for inhibitors which are selective for c-MET and able to target emerging drug-resistant mutants. We report here the discovery, by screening a DNA-encoded chemical library, of a highly selective c-MET inhibitor which was shown by X-ray crystallography to bind to the kinase in an unprecedented manner. These results represent a novel mode of inhibiting c-MET with a small molecule and may provide a route to targeting drug-resistant forms of the kinase whilst avoiding potential toxicity issues associated with broad kinome inhibition. PubMed: 35987508DOI: 10.1016/j.bmcl.2022.128948 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.01 Å) |
Structure validation
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