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. 1995 Jul 27;376(6538):313-20.
doi: 10.1038/376313a0.

Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex

P D Jeffrey  1 , A A Russo, K Polyak, E Gibbs, J Hurwitz, J Massagué, N P Pavletich
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Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex

P D Jeffrey et al. Nature. .

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.

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