Mutational analysis of the vaccinia virus E3 protein defines amino acid residues involved in E3 binding to double-stranded RNA. Export

@article{citeulike:6055403, 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.}, author = {Ho, C. K. and Shuman, S.}, citeulike-article-id = {6055403}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/8642694}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=8642694}, issn = {0022-538X}, journal = {Journal of virology}, keywords = {virology, z-dna}, month = {April}, number = {4}, pages = {2611--2614}, posted-at = {2009-11-02 06:25:37}, priority = {2}, title = {Mutational analysis of the vaccinia virus E3 protein defines amino acid residues involved in E3 binding to double-stranded RNA.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/8642694}, volume = {70}, year = {1996} }

TY - JOUR ID - citeulike:6055403 L3 - citeulike-article-id:6055403 N2 - 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. IS - 4 JF - Journal of virology SN - 0022-538X EP - 2614 TI - Mutational analysis of the vaccinia virus E3 protein defines amino acid residues involved in E3 binding to double-stranded RNA. VL - 70 SP - 2611 KW - virology KW - z-dna AU - Ho, CK AU - Shuman, S PY - 1996/04// UR - http://view.ncbi.nlm.nih.gov/pubmed/8642694 ER -