Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex.
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Jeffrey PD, Russo AA, Polyak K, Gibbs E, Hurwitz J, Massague J, Pavletich NP
Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex.
Nature. 1995 Jul 27;376(6538):313-20.
- PubMed ID
- 7630397 [ View in PubMed]
- Abstract
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.