An analysis of the binding modes of ATP-competitive CDK2 inhibitors as revealed by X-ray structures of protein-inhibitor complexes

Curr Med Chem Anticancer Agents. 2005 Sep;5(5):561-73. doi: 10.2174/1568011054866928.

Abstract

CDK2 is an attractive target for the design of new therapeutic antitumor agent. Numerous CDK2 inhibitors have been discovered and their crystallographic structures either in complex with CDK2 or CDK2/Cyclin A have been published. This review aims to summarize the publicly available structural characterization of CDK2/(Cyclin A) -- ligand complexes and to highlight the similarities among the binding modes of structurally diverse inhibitors.

Publication types

  • Review

MeSH terms

  • Adenosine Triphosphate / chemistry*
  • Adenosine Triphosphate / metabolism
  • Binding, Competitive
  • CDC2-CDC28 Kinases / antagonists & inhibitors*
  • Crystallography, X-Ray
  • Cyclin A / antagonists & inhibitors
  • Cyclin-Dependent Kinase 2
  • Drug Design
  • Enzyme Inhibitors / chemistry*
  • Enzyme Inhibitors / metabolism
  • Humans
  • Ligands
  • Models, Molecular
  • Protein Binding
  • Protein Conformation
  • Structure-Activity Relationship

Substances

  • Cyclin A
  • Enzyme Inhibitors
  • Ligands
  • Adenosine Triphosphate
  • CDC2-CDC28 Kinases
  • CDK2 protein, human
  • Cyclin-Dependent Kinase 2