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Structural characterization of the cyclin-dependent protein kinase family

Lookup NU author(s): Professor Jane Endicott, Professor Martin Noble

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Abstract

Structural studies of members of the CDK (cyclin-dependent protein kinase) family have made a significant contribution to our understanding of the regulation of protein kinases. The structure of monomeric unphosphorylated CDK2 was the first of an inactive protein kinase to be determined and, since then, structures of other members of the CDK family, alone, in complex with regulatory proteins and in differing phosphorylation states, have enhanced our understanding of the molecular mechanisms regulating protein kinase activity. Recently, our knowledge of the structural biology of the CDK family has been extended by determination of structures for members of the transcriptional CDK and CDK-like kinase branches of the extended family. We include these recent structures in the present review and consider them in the light of current models for CDK activation and regulation.


Publication metadata

Author(s): Endicott JA, Noble MEM

Publication type: Article

Publication status: Published

Journal: Biochemical Society Transactions

Year: 2013

Volume: 41

Issue: 4

Pages: 1008-1016

Print publication date: 01/08/2013

ISSN (print): 0300-5127

ISSN (electronic): 1470-8752

Publisher: Portland Press Ltd

URL: http://dx.doi.org/10.1042/BST20130097

DOI: 10.1042/BST20130097


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