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

@article{Jeffrey1995MechanismOC,
  title={Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex},
  author={Philip D. Jeffrey and Alicia A. Russo and Kornelia Polyak and Emily L. Gibbs and Jerard Hurwitz and Joan Massagu{\'e} and Nikola P Pavletich},
  journal={Nature},
  year={1995},
  volume={376},
  pages={313-320}
}
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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