Structural basis of cyclin-dependent kinase activation by phosphorylation View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1996-08-01

AUTHORS

Alicia A. Russo, Philip D. Jeffrey, Nikola P. Pavletich

ABSTRACT

Cyclin-dependent kinase (CDK)–cyclin complexes require phosphorylation on the CDK subunit for full activation of their Ser/Thr protein kinase activity. The crystal structure of the phosphorylated CDK2–CyclinA–ATPγS complex has been determined at 2.6 Å resolution. The phosphate group, which is on the regulatory T-loop of CDK2, is mostly buried, its charge being neutralized by three Arg side chains. The arginines help extend the influence of the phosphate group through a network of hydrogen bonds to both CDK2 and cyclinA. Comparison with the unphosphorylated CDK2–CyclinA complex shows that the T-loop moves by as much as 7 Å, and this affects the putative substrate binding site as well as resulting in additional CDK2–CyclinA contacts. The phosphate group thus acts as a major organizing centre in the CDK2–CyclinA complex. More... »

PAGES

696-700

Journal

TITLE

Nature Structural & Molecular Biology

ISSUE

8

VOLUME

3

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsb0896-696

DOI

http://dx.doi.org/10.1038/nsb0896-696

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1007402396

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8756328


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