Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex
Copyright policy )Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex
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.
- Memorial Sloan Kettering Cancer Center United States
Protein Folding, Binding Sites, Protein Conformation, Cyclin-Dependent Kinase 2, Molecular Sequence Data, Protein Serine-Threonine Kinases, Crystallography, X-Ray, Cyclic AMP-Dependent Protein Kinases, Cyclin-Dependent Kinases, Enzyme Activation, Adenosine Triphosphate, Allosteric Regulation, Cyclins, CDC2-CDC28 Kinases, Computer Graphics, Escherichia coli, Humans, Amino Acid Sequence, Phosphorylation, Protein Binding
Protein Folding, Binding Sites, Protein Conformation, Cyclin-Dependent Kinase 2, Molecular Sequence Data, Protein Serine-Threonine Kinases, Crystallography, X-Ray, Cyclic AMP-Dependent Protein Kinases, Cyclin-Dependent Kinases, Enzyme Activation, Adenosine Triphosphate, Allosteric Regulation, Cyclins, CDC2-CDC28 Kinases, Computer Graphics, Escherichia coli, Humans, Amino Acid Sequence, Phosphorylation, Protein Binding
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