Publication Abstract from PubMed
The crystal structure of the human cyclinA-cyclin-dependent kinase2 (CDK2)-ATP complex has been determined at 2.3 A resolution. CyclinA binds to one side of CDK2's catalytic cleft, inducing large conformational changes in its PSTAIRE helix and T-loop. These changes activate the kinase by realigning active site residues and relieving the steric blockade at the entrance of the catalytic cleft.
Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex.,Jeffrey PD, Russo AA, Polyak K, Gibbs E, Hurwitz J, Massague J, Pavletich NP Nature. 1995 Jul 27;376(6538):313-20. PMID:7630397[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
