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The Structural Basis for Control of Eukaryotic Protein Kinases

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

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Abstract

Eukaryotic protein kinases are key regulators of cell processes. Comparison of the structures of protein kinase domains, both alone and in complexes, allows generalizations to be made about the mechanisms that regulate protein kinase activation. Protein kinases in the active state adopt a catalytically competent conformation upon binding of both the ATP and peptide substrates that has led to an understanding of the catalytic mechanism. Docking sites remote from the catalytic site are a key feature of several substrate recognition complexes. Mechanisms for kinase activation through phosphorylation, additional domains or sub-units, by scaffolding proteins and by kinase dimerization are discussed.


Publication metadata

Author(s): Endicott JA, Noble MEM, Johnson LN

Publication type: Review

Publication status: Published

Journal: Annual Review of Biochemistry

Year: 2012

Volume: 81

Pages: 587-613

Print publication date: 05/04/2012

ISSN (print): 0066-4154

ISSN (electronic): 1545-4509

Publisher: ANNUAL REVIEWS

URL: http://dx.doi.org/10.1146/annurev-biochem-052410-090317

DOI: 10.1146/annurev-biochem-052410-090317


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