Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex.
Jeffrey, Philip D.; Russo, Alicia A.; Polyak, Kornelia; Gibbs, Emma; Hurwitz, Jerard; Massague, Joan; Pavletich, Nikola P.
[Article] Nature. 376(6538):313-320, July 27, 1995.

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The crystal structure of the human cyclinA-cyclin-dependent kinase2 (CDK2)-ATP complex has been determined at 2.3 Angstrom 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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