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Trends Biochem Sci. 2007 Feb;32(2):57-62. Epub 2006 Dec 29.

Activation of PKR: an open and shut case?

Author information

1
Department of Molecular and Cell Biology, 91 N. Eagleville Road, U-3125 University of Connecticut, Storrs, CT 06269, USA. james.cole@uconn.edu

Abstract

The double-stranded (ds) RNA-activated protein kinase, PKR, has a key role in the innate immunity response to viral infection in higher eukaryotes. PKR contains an N-terminal dsRNA-binding domain and a C-terminal kinase domain. In the prevalent autoinhibition model for PKR activation, dsRNA binding induces a conformational change that leads to the release of the dsRNA-binding domain from the kinase, thus relieving the inhibition of the latent enzyme. Structural and biophysical data now favor a model whereby dsRNA principally functions to induce dimerization of PKR via the kinase domain. This dimerization model has implications for other PKR regulatory mechanisms and represents a new structural paradigm for control of protein kinase activity.

PMID:
17196820
PMCID:
PMC2703476
DOI:
10.1016/j.tibs.2006.12.003
[Indexed for MEDLINE]
Free PMC Article

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