Journal
NATURE REVIEWS MOLECULAR CELL BIOLOGY
Volume 8, Issue 7, Pages 530-541Publisher
NATURE PORTFOLIO
DOI: 10.1038/nrm2203
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A typical protein kinase must recognize between one and a few hundred bona fide phosphorylation sites in a background of similar to 700,000 potentially phosphorylatable residues. Multiple mechanisms have evolved that contribute to this exquisite specificity, including the structure of the catalytic site, local and distal interactions between the kinase and substrate, the formation of complexes with scaffolding and adaptor proteins that spatially regulate the kinase, systems-level competition between substrates, and error-correction mechanisms. The responsibility for the recognition of substrates by protein kinases appears to be distributed among a large number of independent, imperfect specificity mechanisms.
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