Browse by author
Lookup NU author(s): Professor Jane Endicott,
Professor Martin NobleORCiD
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
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.
Author(s): Endicott JA, Noble MEM, Johnson LN
Publication type: Review
Publication status: Published
Journal: Annual Review of Biochemistry
Print publication date: 05/04/2012
ISSN (print): 0066-4154
ISSN (electronic): 1545-4509
Publisher: ANNUAL REVIEWS