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. In this article, we review the structural biology work that has led to a precise knowledge of the interactions between CDK2 and small organic molecules binding to its ATP pocket that are determinant for inhibitory activity. The use of this information to design or optimize CDK inhibitors by molecular modeling is also reviewed.
Keywords: X-Ray, Crystallographic, CDK2, Cyclin-Dependent, Anti-Cancer Drug
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