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Dynamics of translational regulation by PKR

Regulation of protein synthesis is a central aspect of cellular response to stimuli. The serine‐threonine kinase PKR is thought to sense the presence of viral RNA during host infection. PKR binds double‐stranded RNA through N‐terminal dsRBD domains, which activates a C‐terminal kinase domain to perform autophosphorylation and phosphorylation of translation initiation factor eIF2alpha. This leads to a global down‐regulation of translation. We have used a variety of structural and biophysical approaches to understand the interplay of RNA binding and kinase activation. Our results provide a global mechanism for PKR structure and function, and underscore the role of dynamics in kinase activation.