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.
Mesh Terms:
Adenosine Triphosphate, Allosteric Regulation, Amino Acid Sequence, Binding Sites, CDC2-CDC28 Kinases, Computer Graphics, Crystallography, X-Ray, Cyclic AMP-Dependent Protein Kinases, Cyclin-Dependent Kinase 2, Cyclin-Dependent Kinases, Cyclins, Enzyme Activation, Escherichia coli, Humans, Molecular Sequence Data, Phosphorylation, Protein Binding, Protein Conformation, Protein Folding, Protein-Serine-Threonine Kinases, Recombinant Proteins, Threonine
Adenosine Triphosphate, Allosteric Regulation, Amino Acid Sequence, Binding Sites, CDC2-CDC28 Kinases, Computer Graphics, Crystallography, X-Ray, Cyclic AMP-Dependent Protein Kinases, Cyclin-Dependent Kinase 2, Cyclin-Dependent Kinases, Cyclins, Enzyme Activation, Escherichia coli, Humans, Molecular Sequence Data, Phosphorylation, Protein Binding, Protein Conformation, Protein Folding, Protein-Serine-Threonine Kinases, Recombinant Proteins, Threonine
Nature
Date: Jul. 27, 1995
PubMed ID: 7630397
View in: Pubmed Google Scholar
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