Journal
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 81
Volume 81, Issue -, Pages 587-613Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev-biochem-052410-090317
Keywords
signal transduction; phosphorylation; substrate recognition; dimerization; pseudokinases
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Funding
- Medical Research Council [G0901526, G0800014] Funding Source: researchfish
- Medical Research Council [G0901526, G0800014] Funding Source: Medline
- MRC [G0800014, G0901526] Funding Source: UKRI
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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.
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