| Literature DB >> 7630397 |
P D Jeffrey1, A A Russo, K Polyak, E Gibbs, J Hurwitz, J Massagué, N P Pavletich.
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.Entities:
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Year: 1995 PMID： 7630397 DOI： 10.1038/376313a0
Source DB: PubMed Journal: Nature ISSN： 0028-0836 Impact factor: 49.962