title: An analysis of the binding modes of ATP-competitive CDK2 inhibitors as revealed by X-ray structures of protein-inhibitor complexes.
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.
authors.affiliation: Department of Chemistry, BU-Oncology, Nerviano Medical Sciences, Via Pasteur, 10, 20014 Nerviano (MI), Italy. anna.vulpetti@nervianoms.com
authors.forename: Anna
authors.initials: A
authors.lastname: Vulpetti
authors.forename: Paolo
authors.initials: P
authors.lastname: Pevarello
mesh_terms: 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
chemical_list: D019925:Cyclin A; D004791:Enzyme Inhibitors; D008024:Ligands; D000255:Adenosine Triphosphate; D042846:CDC2-CDC28 Kinases; C495894:CDK2 protein, human; D051357:Cyclin-Dependent Kinase 2