Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1995-07

AUTHORS

Philip D. Jeffrey, Alicia A. Russo, Kornelia Polyak, Emma Gibbs, Jerard Hurwitz, Joan Massagué, Nikola P. Pavletich

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. More... »

PAGES

313-320

Journal

TITLE

Nature

ISSUE

6538

VOLUME

376

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/376313a0

    DOI

    http://dx.doi.org/10.1038/376313a0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1002475687

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/7630397


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