Cyclin Dependent Kinase 2 (CDK2)
 Ligand in CDK2 ATP-binding site
Ligand in CDK2 ATP-binding site.
Docking example from OTAVAchemicals CDK2 targeted library

The cell division cycle is controlled by cyclin-dependent kinases (cdk), which consist of a catalytic subunit (cdk1-cdk8) and a regulatory subunit (cyclin A-cyclin H). These proteins are regulated in several ways: subunit production, complex formation, (de)phosphorylation, cellular localization, and interaction with various natural protein inhibitors.

Cyclin-dependent kinase 2 (CDK2) plays a critical role in the G1- to S-phase checkpoint of the cell cycle. Like several other protein kinases, CDK2 consists of a relatively small N-terminal domain that is rich in B-sheet structure and a larger C-terminal domain which is predominantly A-helical. The ATP-binding site is located in a pocket between the two domains.

Inhibition of cyclin-dependent kinases is a theme of major interest in current anti-cancer agents research. Different classes of chemical inhibitors of these enzymes have been identified during the past decade and the structural basis of inhibition has been elucidated by X-ray crystallography studies of one member of the family, CDK2. Several types of cdk inhibitors have so far been described: staurosporine, flavopiridole, butyrolactone purine derivatives, indirubin, paullones, and others.

The focused libraries, including docking scores and drug-like properties, are available on request.

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