1CKP
HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR PURVALANOL B
Summary for 1CKP
| Entry DOI | 10.2210/pdb1ckp/pdb |
| Descriptor | PROTEIN (CYCLIN-DEPENDENT PROTEIN KINASE 2), PURVALANOL B, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | protein kinase, cell cycle, phosphorylation, cell division, mitosis, inhibition, hormone-growth factor complex, hormone/growth factor |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 34471.46 |
| Authors | Gray, N.S.,Thunnissen, A.M.W.H.,Schultz, P.G.,Kim, S.H. (deposition date: 1998-07-14, release date: 1999-01-13, Last modification date: 2023-08-09) |
| Primary citation | Gray, N.S.,Wodicka, L.,Thunnissen, A.M.,Norman, T.C.,Kwon, S.,Espinoza, F.H.,Morgan, D.O.,Barnes, G.,LeClerc, S.,Meijer, L.,Kim, S.H.,Lockhart, D.J.,Schultz, P.G. Exploiting chemical libraries, structure, and genomics in the search for kinase inhibitors. Science, 281:533-538, 1998 Cited by PubMed Abstract: Selective protein kinase inhibitors were developed on the basis of the unexpected binding mode of 2,6,9-trisubstituted purines to the adenosine triphosphate-binding site of the human cyclin-dependent kinase 2 (CDK2). By iterating chemical library synthesis and biological screening, potent inhibitors of the human CDK2-cyclin A kinase complex and of Saccharomyces cerevisiae Cdc28p were identified. The structural basis for the binding affinity and selectivity was determined by analysis of a three-dimensional crystal structure of a CDK2-inhibitor complex. The cellular effects of these compounds were characterized in mammalian cells and yeast. In the latter case the effects were characterized on a genome-wide scale by monitoring changes in messenger RNA levels in treated cells with high-density oligonucleotide probe arrays. Purine libraries could provide useful tools for analyzing a variety of signaling and regulatory pathways and may lead to the development of new therapeutics. PubMed: 9677190DOI: 10.1126/science.281.5376.533 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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