1ckp
From Proteopedia
|
HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR PURVALANOL B
Overview
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.
About this Structure
1CKP is a Single protein structure of sequence from Homo sapiens with PVB and EDO as ligands. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
Reference
Exploiting chemical libraries, structure, and genomics in the search for kinase inhibitors., Gray NS, Wodicka L, Thunnissen AM, Norman TC, Kwon S, Espinoza FH, Morgan DO, Barnes G, LeClerc S, Meijer L, Kim SH, Lockhart DJ, Schultz PG, Science. 1998 Jul 24;281(5376):533-8. PMID:9677190
Page seeded by OCA on Mon Nov 12 16:22:54 2007
