2c5o
DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2 PROVIDES INSIGHTS FOR DRUG DESIGN
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OverviewOverview
The cyclin-dependent kinases (CDKs) have been characterized in complex, with a variety of inhibitors, but the majority of structures solved are in, the inactive form. We have solved the structures of six inhibitors in both, the monomeric CDK2 and binary CDK2/cyclinA complexes and demonstrate that, significant differences in ligand binding occur depending on the, activation state. The binding mode of two ligands in particular varies, substantially in active and inactive CDK2. Furthermore, energetic analysis, of CDK2/cyclin/inhibitors demonstrates that a good correlation exists, between the in vitro potency and the calculated energies of interaction, but no such relationship exists for CDK2/inhibitor structures. These, results confirm that monomeric CDK2 ligand complexes do not fully ... [(full description)]
About this StructureAbout this Structure
2C5O is a [Protein complex] structure of sequences from [Homo sapiens] with CK2 as [ligand]. Active as [[1]], with EC number [2.7.1.37]. Full crystallographic information is available from [OCA].
ReferenceReference
Differential binding of inhibitors to active and inactive CDK2 provides insights for drug design., Kontopidis G, McInnes C, Pandalaneni SR, McNae I, Gibson D, Mezna M, Thomas M, Wood G, Wang S, Walkinshaw MD, Fischer PM, Chem Biol. 2006 Feb;13(2):201-11. PMID:16492568
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