<p>Structural and functional characterization of VprBP-UNG2 interface.</p>

<p>(<b>A</b>) Close contacts between UNG2 and VprBP ARM-like domain. Residues involved in close contacts (<a href="plospathogens.org/article/info:doi/10.1371/journal.ppat.1014610#ppat.1014610.s020" target="_blank">S2 Table</a>) are highlighted in orange. (<b>B</b>) Functional validation of the VprBP-UNG2 interface.

Western blot analysis showing that disrupting the contact interface of VprBP N-terminus and UNG2 abolishes Vpr-mediated UNG2 degradation. 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.