Fig. 5. An A291P mutation favors both the closed cryptic pocket in VP35’s IID and increases dsRNA binding.

A DTNB observed labeling rates of both wild-type and the A291P mutation for the two cysteines in the pocket. All four cysteines are present, complete data for all four observed rates are in Supplemental Fig. 4. B Binding of both C247S/C275S and A291P VP35 IID to a fluorescently labeled 25-bp double-stranded RNA. The anisotropy was calculated from measured fluorescence polarization and fit to a single-site binding model (black and orange lines). The means and standard deviations from three replicates are shown but error bars are generally smaller than the symbols. Anisotropy was normalized to the max anisotropy for each dataset. Source data are provided as a Source Data file.