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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenosine Triphosphate / chemistry
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Adenosine Triphosphate / metabolism
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Allosteric Regulation
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Amino Acid Sequence
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Binding Sites
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CDC2-CDC28 Kinases*
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Computer Graphics
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Crystallography, X-Ray
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Cyclic AMP-Dependent Protein Kinases / chemistry
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Cyclin-Dependent Kinase 2
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Cyclin-Dependent Kinases / chemistry*
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Cyclin-Dependent Kinases / metabolism
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Cyclins / chemistry*
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Cyclins / metabolism
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Enzyme Activation
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Escherichia coli
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Humans
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Molecular Sequence Data
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Phosphorylation
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Protein Binding
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Protein Conformation
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Protein Folding
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Protein Serine-Threonine Kinases / chemistry*
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Protein Serine-Threonine Kinases / metabolism
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Recombinant Proteins / chemistry
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Threonine / chemistry
Substances
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Cyclins
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Recombinant Proteins
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Threonine
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Adenosine Triphosphate
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Protein Serine-Threonine Kinases
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Cyclic AMP-Dependent Protein Kinases
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CDC2-CDC28 Kinases
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CDK2 protein, human
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Cyclin-Dependent Kinase 2
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Cyclin-Dependent Kinases