<p>Structural and functional characterization of Vpr C-terminal region.</p>

A difference omit map shows the additional density near helix α2 of Vpr, which is almost parallel to helix α2 and has an average distance of 10 Å to the central axis of helix α2. (<b>B</b>) Functional validation of the Vpr C-terminal mutant.

Western blot analysis showing that the Vpr C-terminal R88A mutant maintains its capacity to degrade UNG2. Western blots were performed in three independent biological replicates (<i>n</i> = 3) with one representative blot shown. Hsp90 was used as an internal loading control.