Mechanism of CDK activation revealed by the struct...[Nature. 1995]

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1: Nature. 1995 Jul 27;376(6538):313-20. Links

Comment in:: Nature. 1995 Jul 27;376(6538):294-5.

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

Jeffrey PD, Russo AA, Polyak K, Gibbs E, Hurwitz J, Massagué J, Pavletich NP.

Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA.

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.

PMID: 7630397 [PubMed - indexed for MEDLINE]

Structural basis of cyclin-dependent kinase activation by phosphorylation. [Nat Struct Biol. 1996]
Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex. [Nature. 1996]
Bound to activate: conformational consequences of cyclin binding to CDK2. [Structure. 1995]
ReviewStructuring cell-cycle biology. [Structure. 1995]
ReviewStructures of staurosporine bound to CDK2 and cAPK--new tools for structure-based design of protein kinase inhibitors. [Structure. 1997]

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

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