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 realig...

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Veröffentlicht in:	Nature (London) 1995-07, Vol.376 (6538), p.313-320
Hauptverfasser:	Jeffrey, Philip D, Russo, Alicia A, Polyak, Kornelia, Gibbs, Emma, Hurwitz, Jerard, Massagué, Joan, Pavletich, Nikola P
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - chemistry Adenosine Triphosphate - metabolism Allosteric Regulation Amino Acid Sequence Analytical, structural and metabolic biochemistry ATP Binding Sites Biochemistry Biological and medical sciences Catalysts CDC2-CDC28 Kinases Cellular biology Computer Graphics Crystalline structure Crystallography Crystallography, X-Ray Cyclic AMP-Dependent Protein Kinases - chemistry Cyclin-Dependent Kinase 2 Cyclin-Dependent Kinases - chemistry Cyclin-Dependent Kinases - metabolism Cyclins - chemistry Cyclins - metabolism Enzyme Activation Enzymes and enzyme inhibitors Escherichia coli Fundamental and applied biological sciences. Psychology Humans Molecular biophysics Molecular Sequence Data Phosphorylation Protein Binding Protein Conformation Protein Folding Protein-Serine-Threonine Kinases - chemistry Protein-Serine-Threonine Kinases - metabolism Proteins Recombinant Proteins - chemistry Structure in molecular biology Threonine - chemistry Transferases
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Zusammenfassung:	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.
ISSN:	0028-0836 1476-4687
DOI:	10.1038/376313a0