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

Article Details

Citation

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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Cyclin-dependent kinase 2P24941Details
Cyclin-A2P20248Details