Activation of PKR: an open and shut case?
Article Details
- CitationCopy to clipboard
Cole JL
Activation of PKR: an open and shut case?
Trends Biochem Sci. 2007 Feb;32(2):57-62. Epub 2006 Dec 29.
- PubMed ID
- 17196820 [ View in PubMed]
- 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.