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

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 t...

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Autores principales:	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
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/f2cad48d7439439680a1cc4a66c3934c
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spelling	oai:doaj.org-article:f2cad48d7439439680a1cc4a66c3934c2021-11-28T12:36:07ZStructure of HIV-1 Vpr in complex with the human nucleotide excision repair protein hHR23A10.1038/s41467-021-27009-w2041-1723https://doaj.org/article/f2cad48d7439439680a1cc4a66c3934c2021-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-27009-whttps://doaj.org/toc/2041-1723Vpr 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.In-Ja L. ByeonGuillermo CaleroYing WuChang H. ByeonJinwon JungMaria DeLuciaXiaohong ZhouSimon WeissJinwoo AhnCaili HaoJacek SkowronskiAngela M. GronenbornNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q 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 Structure of HIV-1 Vpr in complex with the human nucleotide excision repair protein hHR23A
description	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.
format	article
author	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
author_facet	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
author_sort	In-Ja L. Byeon
title	Structure of HIV-1 Vpr in complex with the human nucleotide excision repair protein hHR23A
title_short	Structure of HIV-1 Vpr in complex with the human nucleotide excision repair protein hHR23A
title_full	Structure of HIV-1 Vpr in complex with the human nucleotide excision repair protein hHR23A
title_fullStr	Structure of HIV-1 Vpr in complex with the human nucleotide excision repair protein hHR23A
title_full_unstemmed	Structure of HIV-1 Vpr in complex with the human nucleotide excision repair protein hHR23A
title_sort	structure of hiv-1 vpr in complex with the human nucleotide excision repair protein hhr23a
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/f2cad48d7439439680a1cc4a66c3934c
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Structure of HIV-1 Vpr in complex with the human nucleotide excision repair protein hHR23A

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