Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex
Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex
About this item
Full title
Author / Creator
Publisher
London: Nature Publishing Group UK
Journal title
Language
English
Formats
Publication information
Publisher
London: Nature Publishing Group UK
Subjects
More information
Scope and Contents
Contents
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 bloc...
Alternative Titles
Full title
Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex
Authors, Artists and Contributors
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_proquest_miscellaneous_77431829
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_77431829
Other Identifiers
ISSN
0028-0836
E-ISSN
1476-4687
DOI
10.1038/376313a0
