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.
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Jeffrey, P., Russo, A., Polyak, K. et al. Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex. Nature 376, 313–320 (1995). https://doi.org/10.1038/376313a0
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DOI: https://doi.org/10.1038/376313a0
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