An analysis of the binding modes of ATP-competitive CDK2 inhibitors as revealed by X-ray structures of protein-inhibitor complexes.
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.
Vulpetti
Anna
A
Department of Chemistry, BU-Oncology, Nerviano Medical Sciences, Via Pasteur, 10, 20014 Nerviano (MI), Italy. anna.vulpetti@nervianoms.com
Pevarello
Paolo
P
D000255:Adenosine Triphosphate / Q000737:chemistry* / Q000378:metabolism; D001667:Binding, Competitive; D042846:CDC2-CDC28 Kinases / Q000037:antagonists & inhibitors*; D018360:Crystallography, X-Ray; D019925:Cyclin A / Q000037:antagonists & inhibitors; D051357:Cyclin-Dependent Kinase 2; D015195:Drug Design; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008024:Ligands; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D019925:Cyclin A; D004791:Enzyme Inhibitors; D008024:Ligands; D000255:Adenosine Triphosphate; D042846:CDC2-CDC28 Kinases; C495894:CDK2 protein, human; D051357:Cyclin-Dependent Kinase 2