2OH4
Crystal structure of Vegfr2 with a benzimidazole-urea inhibitor
Summary for 2OH4
| Entry DOI | 10.2210/pdb2oh4/pdb |
| Related | 1vr2 1y6a 1y6b 1ywm |
| Descriptor | Vascular endothelial growth factor receptor 2, SULFATE ION, METHYL (5-{4-[({[2-FLUORO-5-(TRIFLUOROMETHYL)PHENYL]AMINO}CARBONYL)AMINO]PHENOXY}-1H-BENZIMIDAZOL-2-YL)CARBAMATE, ... (4 entities in total) |
| Functional Keywords | vascular endothelial growth factor receptor 2, tyrosine-protein kinase, angiogenesis, atp-binding, phosphorylation, kinase insert domain receptor, protein-tyrosine kinase receptor flk-1, transferase |
| Biological source | Homo sapiens (Human) More |
| Cellular location | Cell junction . Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted . Isoform 3: Secreted: P35968 |
| Total number of polymer chains | 1 |
| Total formula weight | 37104.21 |
| Authors | Nolte, R.T.,Wang, L. (deposition date: 2007-01-09, release date: 2007-09-18, Last modification date: 2024-10-16) |
| Primary citation | Hasegawa, M.,Nishigaki, N.,Washio, Y.,Kano, K.,Harris, P.A.,Sato, H.,Mori, I.,West, R.I.,Shibahara, M.,Toyoda, H.,Wang, L.,Nolte, R.T.,Veal, J.M.,Cheung, M. Discovery of Novel Benzimidazoles as Potent Inhibitors of TIE-2 and VEGFR-2 Tyrosine Kinase Receptors. J.Med.Chem., 50:4453-4470, 2007 Cited by PubMed Abstract: We herein disclose a novel chemical series of benzimidazole-ureas as inhibitors of VEGFR-2 and TIE-2 kinase receptors, both of which are implicated in angiogenesis. Structure-activity relationship (SAR) studies elucidated a critical role for the N1 nitrogen of both the benzimidazole (segment E) and urea (segment B) moieties. The SAR results were also supported by the X-ray crystallographic elucidation of the role of the N1 nitrogen and the urea moiety when the benzimidazole-urea compounds were bound to the VEGFR-2 enzyme. The left side phenyl ring (segment A) occupies the backpocket where a 3-hydrophobic substituent was favored for TIE-2 activity. PubMed: 17676829DOI: 10.1021/jm0611051 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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