Nature Communications (Nov 2021)

Structure of HIV-1 Vpr in complex with the human nucleotide excision repair protein hHR23A

  • In-Ja L. Byeon,
  • Guillermo Calero,
  • Ying Wu,
  • Chang H. Byeon,
  • Jinwon Jung,
  • Maria DeLucia,
  • Xiaohong Zhou,
  • Simon Weiss,
  • Jinwoo Ahn,
  • Caili Hao,
  • Jacek Skowronski,
  • Angela M. Gronenborn

DOI
https://doi.org/10.1038/s41467-021-27009-w
Journal volume & issue
Vol. 12, no. 1
pp. 1 – 13

Abstract

Read online

Vpr is a HIV-1 accessory virulence factor that also interacts with the human DNA repair protein hHR23A. Here, the authors present the structure of Vpr in complex with the C-terminal half of hHR23A comprising the XPC-binding and ubiquitin-associated domains, which reveals that hHR23A interacts with the DCAF1-binding and not the substrate-binding Vpr surface and further illustrates how Vpr acts as a versatile structural adapter that targets diverse DNA repair pathways.