Understanding the structural basis of HIV-1 restriction by the full length double-domain APOBEC3G

APOBEC3G (A3G) belongs to the DNA/RNA cytosine deaminase family that plays important roles in innate immunity against HIV and internal retroelements. Here the authors report the structures of two full-length A3G variants that provides insight into domain organization, multimerization, RNA binding, a...

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Autores principales:	Hanjing Yang, Fumiaki Ito, Aaron D. Wolfe, Shuxing Li, Nazanin Mohammadzadeh, Robin P. Love, Maocai Yan, Brett Zirkle, Amit Gaba, Linda Chelico, Xiaojiang S. Chen
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/81810bdeadd84813b61a8392fef16fb6
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spelling	oai:doaj.org-article:81810bdeadd84813b61a8392fef16fb62021-12-02T15:39:16ZUnderstanding the structural basis of HIV-1 restriction by the full length double-domain APOBEC3G10.1038/s41467-020-14377-y2041-1723https://doaj.org/article/81810bdeadd84813b61a8392fef16fb62020-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-14377-yhttps://doaj.org/toc/2041-1723APOBEC3G (A3G) belongs to the DNA/RNA cytosine deaminase family that plays important roles in innate immunity against HIV and internal retroelements. Here the authors report the structures of two full-length A3G variants that provides insight into domain organization, multimerization, RNA binding, and viral restriction.Hanjing YangFumiaki ItoAaron D. WolfeShuxing LiNazanin MohammadzadehRobin P. LoveMaocai YanBrett ZirkleAmit GabaLinda ChelicoXiaojiang S. ChenNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Hanjing Yang Fumiaki Ito Aaron D. Wolfe Shuxing Li Nazanin Mohammadzadeh Robin P. Love Maocai Yan Brett Zirkle Amit Gaba Linda Chelico Xiaojiang S. Chen Understanding the structural basis of HIV-1 restriction by the full length double-domain APOBEC3G
description	APOBEC3G (A3G) belongs to the DNA/RNA cytosine deaminase family that plays important roles in innate immunity against HIV and internal retroelements. Here the authors report the structures of two full-length A3G variants that provides insight into domain organization, multimerization, RNA binding, and viral restriction.
format	article
author	Hanjing Yang Fumiaki Ito Aaron D. Wolfe Shuxing Li Nazanin Mohammadzadeh Robin P. Love Maocai Yan Brett Zirkle Amit Gaba Linda Chelico Xiaojiang S. Chen
author_facet	Hanjing Yang Fumiaki Ito Aaron D. Wolfe Shuxing Li Nazanin Mohammadzadeh Robin P. Love Maocai Yan Brett Zirkle Amit Gaba Linda Chelico Xiaojiang S. Chen
author_sort	Hanjing Yang
title	Understanding the structural basis of HIV-1 restriction by the full length double-domain APOBEC3G
title_short	Understanding the structural basis of HIV-1 restriction by the full length double-domain APOBEC3G
title_full	Understanding the structural basis of HIV-1 restriction by the full length double-domain APOBEC3G
title_fullStr	Understanding the structural basis of HIV-1 restriction by the full length double-domain APOBEC3G
title_full_unstemmed	Understanding the structural basis of HIV-1 restriction by the full length double-domain APOBEC3G
title_sort	understanding the structural basis of hiv-1 restriction by the full length double-domain apobec3g
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/81810bdeadd84813b61a8392fef16fb6
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Understanding the structural basis of HIV-1 restriction by the full length double-domain APOBEC3G

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