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Nat Rev Mol Cell Biol. 2012 Oct;13(10):646-58. doi: 10.1038/nrm3432. Epub 2012 Sep 20.

Assembly of allosteric macromolecular switches: lessons from PKA.

Author information

1
Department of Pharmacology, University of California, San Diego, La Jolla, 92093-90654, USA. staylor@ucsd.edu

Abstract

Protein kinases are dynamic molecular switches that have evolved to be only transiently activated. Kinase activity is embedded within a conserved kinase core, which is typically regulated by associated domains, linkers and interacting proteins. Moreover, protein kinases are often tethered to large macromolecular complexes to provide tighter spatiotemporal control. Thus, structural characterization of kinase domains alone is insufficient to explain protein kinase function and regulation in vivo. Recent progress in structural characterization of cyclic AMP-dependent protein kinase (PKA) exemplifies how our knowledge of kinase signalling has evolved by shifting the focus of structural studies from single kinase subunits to macromolecular complexes.

PMID:
22992589
PMCID:
PMC3985763
DOI:
10.1038/nrm3432
[Indexed for MEDLINE]
Free PMC Article
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