4BRX
Focal Adhesion Kinase catalytic domain in complex with a diarylamino- 1,3,5-triazine inhibitor
Summary for 4BRX
| Entry DOI | 10.2210/pdb4brx/pdb |
| Descriptor | FOCAL ADHESION KINASE 1, 2-(4-(2-methoxy-4-morpholinophenylamino)-1,3,5-triazin-2-ylamino)-N-methylbenzamide, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | transferase, kinase inhibitor, atp-binding, integrin signaling |
| Biological source | GALLUS GALLUS (CHICKEN) |
| Total number of polymer chains | 1 |
| Total formula weight | 32263.35 |
| Authors | Le Coq, J.,Lietha, D. (deposition date: 2013-06-05, release date: 2013-07-24, Last modification date: 2023-12-20) |
| Primary citation | Dao, P.,Jarray, R.,Le Coq, J.,Lietha, D.,Loukaci, A.,Lepelletier, Y.,Hadj-Slimane, R.,Garbay, C.,Raynaud, F.,Chen, H. Synthesis of Novel Diarylamino-1,3,5-Triazine Derivatives as Fak Inhibitors with Anti-Angiogenic Activity. Bioorg.Med.Chem.Lett., 23:4552-, 2013 Cited by PubMed Abstract: We report herein the synthesis of novel diarylamino-1,3,5-triazine derivatives as FAK (focal adhesion kinase) inhibitors and the evaluation of their anti-angiogenic activity on HUVEC cells. Generally, the effects of these compounds on endothelial cells could be correlated with their kinase inhibitory activity. The most efficient compounds displayed inhibition of viability against HUVEC cells in the micromolar range, as observed with TAE-226, which was designed by Novartis Pharma AG. X-ray crystallographic analysis of the co-crystal structure for compound 34 revealed that the mode of interaction with the FAK kinase domain is highly similar to that observed in the complex of TAE-226. PubMed: 23845217DOI: 10.1016/J.BMCL.2013.06.038 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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