期刊
TRENDS IN BIOCHEMICAL SCIENCES
卷 32, 期 2, 页码 57-62出版社
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2006.12.003
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资金
- NIAID NIH HHS [AI 53615, R01 AI053615-05, R01 AI053615] Funding Source: Medline
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.
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