1fin: Difference between revisions
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==Overview== | ==Overview== | ||
The crystal structure of the human cyclinA-cyclin-dependent kinase2 | 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Jeffrey, P | [[Category: Jeffrey, P D.]] | ||
[[Category: Pavletich, N | [[Category: Pavletich, N P.]] | ||
[[Category: Russo, A | [[Category: Russo, A A.]] | ||
[[Category: ATP]] | [[Category: ATP]] | ||
[[Category: cdk]] | [[Category: cdk]] | ||
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[[Category: phosphorylation]] | [[Category: phosphorylation]] | ||
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Revision as of 13:39, 21 February 2008
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CYCLIN A-CYCLIN-DEPENDENT KINASE 2 COMPLEX
OverviewOverview
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.
About this StructureAbout this Structure
1FIN is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex., Jeffrey PD, Russo AA, Polyak K, Gibbs E, Hurwitz J, Massague J, Pavletich NP, Nature. 1995 Jul 27;376(6538):313-20. PMID:7630397
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