1fin: Difference between revisions

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==Overview==
==Overview==
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.
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.D.]]
[[Category: Jeffrey, P D.]]
[[Category: Pavletich, N.P.]]
[[Category: Pavletich, N P.]]
[[Category: Russo, A.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

File:1fin.jpg


1fin, resolution 2.3Å

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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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