Structural basis of transmembrane coupling of the HIV-1 envelope glycoprotein

HIV-1 envelope glycoprotein (Env) mediates the fusion of viral and target cell membranes and is a major target for HIV vaccine development. Here, the authors determine the NMR structure of a bicelle incorporated Env segment comprising the transmembrane domain (TMD) and a portion of the cytoplasmic t...

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Autores principales:	Alessandro Piai, Qingshan Fu, Yongfei Cai, Fadi Ghantous, Tianshu Xiao, Md Munan Shaik, Hanqin Peng, Sophia Rits-Volloch, Wen Chen, Michael S. Seaman, Bing Chen, James J. Chou
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/e13057d2254f431aa52b8fc7024ffbdf
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spelling	oai:doaj.org-article:e13057d2254f431aa52b8fc7024ffbdf2021-12-02T14:41:13ZStructural basis of transmembrane coupling of the HIV-1 envelope glycoprotein10.1038/s41467-020-16165-02041-1723https://doaj.org/article/e13057d2254f431aa52b8fc7024ffbdf2020-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-16165-0https://doaj.org/toc/2041-1723HIV-1 envelope glycoprotein (Env) mediates the fusion of viral and target cell membranes and is a major target for HIV vaccine development. Here, the authors determine the NMR structure of a bicelle incorporated Env segment comprising the transmembrane domain (TMD) and a portion of the cytoplasmic tail (CT), and show that the CT folds into membrane attached amphipathic helices that wrap around the TMD thereby forming a support baseplate for the rest of Env, and they also provide insights into the dynamic coupling across the TMD between the ectodomain and CT.Alessandro PiaiQingshan FuYongfei CaiFadi GhantousTianshu XiaoMd Munan ShaikHanqin PengSophia Rits-VollochWen ChenMichael S. SeamanBing ChenJames J. ChouNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Alessandro Piai Qingshan Fu Yongfei Cai Fadi Ghantous Tianshu Xiao Md Munan Shaik Hanqin Peng Sophia Rits-Volloch Wen Chen Michael S. Seaman Bing Chen James J. Chou Structural basis of transmembrane coupling of the HIV-1 envelope glycoprotein
description	HIV-1 envelope glycoprotein (Env) mediates the fusion of viral and target cell membranes and is a major target for HIV vaccine development. Here, the authors determine the NMR structure of a bicelle incorporated Env segment comprising the transmembrane domain (TMD) and a portion of the cytoplasmic tail (CT), and show that the CT folds into membrane attached amphipathic helices that wrap around the TMD thereby forming a support baseplate for the rest of Env, and they also provide insights into the dynamic coupling across the TMD between the ectodomain and CT.
format	article
author	Alessandro Piai Qingshan Fu Yongfei Cai Fadi Ghantous Tianshu Xiao Md Munan Shaik Hanqin Peng Sophia Rits-Volloch Wen Chen Michael S. Seaman Bing Chen James J. Chou
author_facet	Alessandro Piai Qingshan Fu Yongfei Cai Fadi Ghantous Tianshu Xiao Md Munan Shaik Hanqin Peng Sophia Rits-Volloch Wen Chen Michael S. Seaman Bing Chen James J. Chou
author_sort	Alessandro Piai
title	Structural basis of transmembrane coupling of the HIV-1 envelope glycoprotein
title_short	Structural basis of transmembrane coupling of the HIV-1 envelope glycoprotein
title_full	Structural basis of transmembrane coupling of the HIV-1 envelope glycoprotein
title_fullStr	Structural basis of transmembrane coupling of the HIV-1 envelope glycoprotein
title_full_unstemmed	Structural basis of transmembrane coupling of the HIV-1 envelope glycoprotein
title_sort	structural basis of transmembrane coupling of the hiv-1 envelope glycoprotein
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/e13057d2254f431aa52b8fc7024ffbdf
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Structural basis of transmembrane coupling of the HIV-1 envelope glycoprotein

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