Role of the Interdomain Linker in RNA-Activated Protein Kinase Activation.
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ABSTRACT:
SUBMITTER: Husain B
PROVIDER: S-EPMC4718896 | biostudies-literature | 2016 Jan
REPOSITORIES: biostudies-literature
Publications
Role of the Interdomain Linker in RNA-Activated Protein Kinase Activation.
Husain Bushra B Mayo Christopher C Cole James L JL
Biochemistry 20151230 2
RNA-activated protein kinase (PKR) is a key component of the interferon-induced antiviral pathway in higher eukaryotes. Upon recognition of viral dsRNA, PKR is activated via dimerization and autophosphorylation. PKR contains two N-terminal dsRNA binding domains (dsRBD) and a C-terminal kinase domain. The dsRBDs and the kinase are separated by a long, unstructured ∼80-amino acid linker in the human enzyme. The length of the N-terminal portion of the linker varies among PKR sequences, and it is co ...[more]
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