4YVE
ROCK 1 bound to methoxyphenyl thiazole inhibitor
Summary for 4YVE
| Entry DOI | 10.2210/pdb4yve/pdb |
| Related | 4YVC |
| Descriptor | Rho-associated protein kinase 1, 2-(3-methoxyphenyl)-N-[4-(pyridin-4-yl)-1,3-thiazol-2-yl]acetamide (3 entities in total) |
| Functional Keywords | kinase, dimer, dimerization, myosin, transferase-transferase inhibitor complex, transferase/transferase inhibitor |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 96675.34 |
| Authors | Jacobs, M.D. (deposition date: 2015-03-19, release date: 2015-06-10, Last modification date: 2023-09-27) |
| Primary citation | Green, J.,Cao, J.,Bandarage, U.K.,Gao, H.,Court, J.,Marhefka, C.,Jacobs, M.,Taslimi, P.,Newsome, D.,Nakayama, T.,Shah, S.,Rodems, S. Design, Synthesis, and Structure-Activity Relationships of Pyridine-Based Rho Kinase (ROCK) Inhibitors. J.Med.Chem., 58:5028-5037, 2015 Cited by PubMed Abstract: The Rho kinases (ROCK1 and ROCK2) are highly homologous serine/threonine kinases that act on substrates associated with cellular motility, morphology, and contraction and are of therapeutic interest in diseases associated with cellular migration and contraction, such as hypertension, glaucoma, and erectile dysfunction. Beginning with compound 4, an inhibitor of ROCK1 identified through high-throughput screening, systematic exploration of SAR, and application of structure-based design, led to potent and selective ROCK inhibitors. Compound 37 represents significant improvements in inhibition potency, kinase selectivity, and CYP inhibition and possesses pharmacokinetics suitable for in vivo experimentation. PubMed: 26039570DOI: 10.1021/acs.jmedchem.5b00424 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.4 Å) |
Structure validation
Download full validation report
