Mutational Analysis of the Double-stranded RNA (dsRNA) Binding Domain of the dsRNA-activated Protein Kinase, PKR (∗)

• Published in: The Journal of biological chemistry Vol. 270; no. 6; pp. 2601 - 2606
• Main Authors: McMillan, Nigel A.J., Carpick, Bruce W., Hollis, Britton, Toone, W. Mark, Zamanian-Daryoush, Maryam, Williams, Bryan R.G.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 10.02.1995; American Society for Biochemistry and Molecular Biology
• Subjects: 3T3 Cells; Alanine - genetics; Alanine - metabolism; Amino Acid Sequence; Animals; Base Sequence; Cloning, Molecular; eIF-2 Kinase; Humans; Mice; Molecular Sequence Data; Mutagenesis; Mutation; Protein Binding; Protein-Serine-Threonine Kinases - genetics; Protein-Serine-Threonine Kinases - metabolism; RNA, Double-Stranded - metabolism; Saccharomyces cerevisiae - genetics; Sequence Homology, Amino Acid

The interferon-induced, double-stranded RNA (dsRNA)-dependent protein kinase, PKR, is an inhibitor of translation and has antiviral, antiproliferative, and antitumor properties. Previously, the dsRNA binding domain had been located within the N-terminal region of PKR and subsequently shown to includ...