Mutational analysis of the vaccinia virus E3 protein defines amino acid residues involved in E3 binding to double-stranded RNA Journal Article
| Authors: | Ho, C. K.; Shuman, S. |
| Article Title: | Mutational analysis of the vaccinia virus E3 protein defines amino acid residues involved in E3 binding to double-stranded RNA |
| Abstract: | Alanine-substitution mutations were targeted to 14 amino acid residues within the double-stranded (ds) RNA binding motif (dsRBM) of the vaccinia virus E3 protein. Substitutions at six positions-Glu-124, Phe-135, Phe-148, Lys-167, Arg-168, and Lys-171-caused significant reductions in dsRNA binding. These six residues are conserved in the two dsRBMs for which structural information is available (Escherichia coli RNase III and Drosophila melanogaster staufen) and in many other members of the dsRBM protein family. Residues we show to be important for dsRNA binding by vaccinia virus E3 map to the same face of the dsRBM structure and are thus likely to compose part of the RNA binding site. |
| Keywords: | controlled study; nonhuman; animals; amino acid substitution; structure activity relation; rna binding protein; rna-binding proteins; amino acid sequence; molecular sequence data; escherichia coli; vaccinia virus; mutagenesis, site-directed; binding sites; drosophila melanogaster; sequence homology; double stranded rna; ribonuclease iii; rna, double-stranded; viral proteins; protein rna binding; priority journal; article |
| Journal Title: | Journal of Virology |
| Volume: | 70 |
| Issue: | 4 |
| ISSN: | 0022-538X |
| Publisher: | American Society for Microbiology |
| Date Published: | 1996-04-01 |
| Start Page: | 2611 |
| End Page: | 2614 |
| Language: | English |
| PUBMED: | 8642694 |
| PROVIDER: | scopus |
| PMCID: | PMC190110 |
| DOI/URL: | |
| Notes: | Article -- Export Date: 22 November 2017 -- Source: Scopus |
