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- W4244482783 abstract "The RNA-activated protein kinase, PKR, is a key mediator of the innate immunity response to viral infection. Viral double-stranded RNAs induce PKR dimerization and autophosphorylation. The PKR kinase domain forms a back-to-back dimer. However, intermolecular (trans) autophosphorylation is not feasible in this arrangement. We have obtained PKR kinase structures that resolves this dilemma. The kinase protomers interact via the known back-to-back interface as well as a front-to-front interface that is formed by exchange of activation segments. Mutational analysis of the front-to-front interface support a functional role in PKR activation. Molecular dynamics simulations reveal that the activation segment is highly dynamic in the front-to-front dimer and can adopt conformations conducive to phosphoryl transfer. We propose a mechanism where back-to-back dimerization induces a conformational change that activates PKR to phosphorylate a “substrate” kinase docked in a front-to-front geometry. This mechanism may be relevant to related kinases that phosphorylate the eukaryotic initiation factor eIF2α." @default.
- W4244482783 created "2022-05-12" @default.
- W4244482783 creator A5007254483 @default.
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- W4244482783 creator A5056911359 @default.
- W4244482783 creator A5059516347 @default.
- W4244482783 creator A5091638725 @default.
- W4244482783 date "2019-06-17" @default.
- W4244482783 modified "2023-10-13" @default.
- W4244482783 title "Structural Basis of Protein Kinase R Autophosphorylation" @default.
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- W4244482783 doi "https://doi.org/10.1021/acs.biochem.9b00161" @default.
- W4244482783 hasPublicationYear "2019" @default.
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