Mechanistic Link between PKR Dimerization, Autophosphorylation, and eIF2α Substrate Recognition

@article{Dey2005MechanisticLB,
  title={Mechanistic Link between PKR Dimerization, Autophosphorylation, and eIF2α Substrate Recognition},
  author={Madhusudan Dey and Chune Cao and Arvin C. Dar and Tomohiko Tamura and Keiko Ozato and Frank Sicheri and Thomas E. Dever},
  journal={Cell},
  year={2005},
  volume={122},
  pages={901-913}
}
The antiviral protein kinase PKR inhibits protein synthesis by phosphorylating the translation initiation factor eIF2alpha on Ser51. Binding of double-stranded RNA to the regulatory domains of PKR promotes dimerization, autophosphorylation, and the functional activation of the kinase. Herein, we identify mutations that activate PKR in the absence of its regulatory domains and map the mutations to a recently identified dimerization surface on the kinase catalytic domain. Mutations of other… CONTINUE READING