Fig. 5: hHR23A is displaced from the Vpr/hHR23A complex by DCAF1.
From: Structure of HIV-1 Vpr in complex with the human nucleotide excision repair protein hHR23A
Analytical gel-filtration chromatography elution profiles of a DCAF11057–1396, b hHR23AFL, c the Vpr1–79/hHR23AFL complex, d an equimolar mixture of the Vpr1–79/hHR23AFL complex and DCAF11057–1396 and e SDS–PAGE analysis of the elution peaks; Lane numbers correspond to peak numbers in (a–d). Analytical gel-filtration chromatography elution profiles of f hHR23AFL, g the VprFL/hHR23AFL complex, h UNG2, i an equimolar mixture of hHR23AFL and UNG2, j an equimolar mixture of the VprFL/hHR23AFL complex and UNG2 and k SDS–PAGE analysis of the elution peaks. Lane numbers correspond to peak numbers in (f–j). Two independent experiments were performed yielding similar results. l, m Molecular model of the UNG2/Vpr1–79/hHR23A223–363 complex based on the superposition of the UNG2/Vpr1–79/DCAF11045–1396 complex and the current Vpr1–79–L-hHR23A223–363 complex without (l) and with displaying DCAF1 (m). n Surface representation of Vpr1–79 in two views, highlighting residues with DCAF11045–1396 contacts (blue), with both DCAF11045–1396 and hHR23A223–363 contacts (silver), and with hHR23A223–363 UBA2 only contacts (olive). Vpr1–79 residues that do not interact with DCAF11045–1396 or hHR23A223–363 are shown in red.
