Structural and functional analyses of hepatitis B virus X protein BH3-like domain and Bcl-xL interaction

Hepatitis B virus X protein (HBx) binds anti-apoptotic Bcl-xL through its BH3-like motif to promote viral replication. Here, the authors provide the structure of the HBx BH3-like domain and Bcl-xL, which shows an unusual mode of interaction, and identify a short peptide that inhibits HBV replication...

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Autores principales: Tian-Ying Zhang, Hong-Ying Chen, Jia-Li Cao, Hua-Long Xiong, Xiao-Bing Mo, Tian-Liang Li, Xiao-Zhen Kang, Jing-Hua Zhao, Bo Yin, Xiang Zhao, Cheng-Hao Huang, Quan Yuan, Ding Xue, Ning-Shao Xia, Y. Adam Yuan
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Lenguaje:EN
Publicado: Nature Portfolio 2019
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Acceso en línea:https://doaj.org/article/bccf1b6cc6fc4a3986b958df99dc247d
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spelling oai:doaj.org-article:bccf1b6cc6fc4a3986b958df99dc247d2021-12-02T16:58:27ZStructural and functional analyses of hepatitis B virus X protein BH3-like domain and Bcl-xL interaction10.1038/s41467-019-11173-12041-1723https://doaj.org/article/bccf1b6cc6fc4a3986b958df99dc247d2019-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-11173-1https://doaj.org/toc/2041-1723Hepatitis B virus X protein (HBx) binds anti-apoptotic Bcl-xL through its BH3-like motif to promote viral replication. Here, the authors provide the structure of the HBx BH3-like domain and Bcl-xL, which shows an unusual mode of interaction, and identify a short peptide that inhibits HBV replication in cultured human hepatic cells.Tian-Ying ZhangHong-Ying ChenJia-Li CaoHua-Long XiongXiao-Bing MoTian-Liang LiXiao-Zhen KangJing-Hua ZhaoBo YinXiang ZhaoCheng-Hao HuangQuan YuanDing XueNing-Shao XiaY. Adam YuanNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Tian-Ying Zhang
Hong-Ying Chen
Jia-Li Cao
Hua-Long Xiong
Xiao-Bing Mo
Tian-Liang Li
Xiao-Zhen Kang
Jing-Hua Zhao
Bo Yin
Xiang Zhao
Cheng-Hao Huang
Quan Yuan
Ding Xue
Ning-Shao Xia
Y. Adam Yuan
Structural and functional analyses of hepatitis B virus X protein BH3-like domain and Bcl-xL interaction
description Hepatitis B virus X protein (HBx) binds anti-apoptotic Bcl-xL through its BH3-like motif to promote viral replication. Here, the authors provide the structure of the HBx BH3-like domain and Bcl-xL, which shows an unusual mode of interaction, and identify a short peptide that inhibits HBV replication in cultured human hepatic cells.
format article
author Tian-Ying Zhang
Hong-Ying Chen
Jia-Li Cao
Hua-Long Xiong
Xiao-Bing Mo
Tian-Liang Li
Xiao-Zhen Kang
Jing-Hua Zhao
Bo Yin
Xiang Zhao
Cheng-Hao Huang
Quan Yuan
Ding Xue
Ning-Shao Xia
Y. Adam Yuan
author_facet Tian-Ying Zhang
Hong-Ying Chen
Jia-Li Cao
Hua-Long Xiong
Xiao-Bing Mo
Tian-Liang Li
Xiao-Zhen Kang
Jing-Hua Zhao
Bo Yin
Xiang Zhao
Cheng-Hao Huang
Quan Yuan
Ding Xue
Ning-Shao Xia
Y. Adam Yuan
author_sort Tian-Ying Zhang
title Structural and functional analyses of hepatitis B virus X protein BH3-like domain and Bcl-xL interaction
title_short Structural and functional analyses of hepatitis B virus X protein BH3-like domain and Bcl-xL interaction
title_full Structural and functional analyses of hepatitis B virus X protein BH3-like domain and Bcl-xL interaction
title_fullStr Structural and functional analyses of hepatitis B virus X protein BH3-like domain and Bcl-xL interaction
title_full_unstemmed Structural and functional analyses of hepatitis B virus X protein BH3-like domain and Bcl-xL interaction
title_sort structural and functional analyses of hepatitis b virus x protein bh3-like domain and bcl-xl interaction
publisher Nature Portfolio
publishDate 2019
url https://doaj.org/article/bccf1b6cc6fc4a3986b958df99dc247d
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