Unknown

Dataset Information

0

Activation of PKR: an open and shut case?


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.

SUBMITTER: Cole JL 

PROVIDER: S-EPMC2703476 | biostudies-literature | 2007 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

Activation of PKR: an open and shut case?

Cole James L JL  

Trends in biochemical sciences 20061229 2


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 m  ...[more]

Similar Datasets

| S-EPMC2699264 | biostudies-literature
| S-EPMC5029964 | biostudies-literature
| S-EPMC3615642 | biostudies-literature
| S-EPMC3504668 | biostudies-literature
| S-EPMC8153938 | biostudies-literature
| S-EPMC7405929 | biostudies-literature
| S-EPMC2763119 | biostudies-literature
| S-EPMC2926283 | biostudies-literature
| S-EPMC2868028 | biostudies-literature
| S-EPMC400457 | biostudies-literature