Capturing the inherent structural dynamics of the HIV-1 envelope glycoprotein fusion peptide

The fusion peptide (FP) of HIV envelope (Env) is critical in the cell entry process. Here, Kumar et al. present crystal structures of B41 SOSIP.664 Env trimer and show the dynamic nature of the FP and proximal region, which likely relates to conformational rearrangements required for membrane fusion...

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Autores principales:	Sonu Kumar, Anita Sarkar, Pavel Pugach, Rogier W. Sanders, John P. Moore, Andrew B. Ward, Ian A. Wilson
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/422d5a067ce54af08da13e4b5373a101
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spelling	oai:doaj.org-article:422d5a067ce54af08da13e4b5373a1012021-12-02T15:35:39ZCapturing the inherent structural dynamics of the HIV-1 envelope glycoprotein fusion peptide10.1038/s41467-019-08738-52041-1723https://doaj.org/article/422d5a067ce54af08da13e4b5373a1012019-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-08738-5https://doaj.org/toc/2041-1723The fusion peptide (FP) of HIV envelope (Env) is critical in the cell entry process. Here, Kumar et al. present crystal structures of B41 SOSIP.664 Env trimer and show the dynamic nature of the FP and proximal region, which likely relates to conformational rearrangements required for membrane fusion.Sonu KumarAnita SarkarPavel PugachRogier W. SandersJohn P. MooreAndrew B. WardIan A. WilsonNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Sonu Kumar Anita Sarkar Pavel Pugach Rogier W. Sanders John P. Moore Andrew B. Ward Ian A. Wilson Capturing the inherent structural dynamics of the HIV-1 envelope glycoprotein fusion peptide
description	The fusion peptide (FP) of HIV envelope (Env) is critical in the cell entry process. Here, Kumar et al. present crystal structures of B41 SOSIP.664 Env trimer and show the dynamic nature of the FP and proximal region, which likely relates to conformational rearrangements required for membrane fusion.
format	article
author	Sonu Kumar Anita Sarkar Pavel Pugach Rogier W. Sanders John P. Moore Andrew B. Ward Ian A. Wilson
author_facet	Sonu Kumar Anita Sarkar Pavel Pugach Rogier W. Sanders John P. Moore Andrew B. Ward Ian A. Wilson
author_sort	Sonu Kumar
title	Capturing the inherent structural dynamics of the HIV-1 envelope glycoprotein fusion peptide
title_short	Capturing the inherent structural dynamics of the HIV-1 envelope glycoprotein fusion peptide
title_full	Capturing the inherent structural dynamics of the HIV-1 envelope glycoprotein fusion peptide
title_fullStr	Capturing the inherent structural dynamics of the HIV-1 envelope glycoprotein fusion peptide
title_full_unstemmed	Capturing the inherent structural dynamics of the HIV-1 envelope glycoprotein fusion peptide
title_sort	capturing the inherent structural dynamics of the hiv-1 envelope glycoprotein fusion peptide
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/422d5a067ce54af08da13e4b5373a101
work_keys_str_mv	AT sonukumar capturingtheinherentstructuraldynamicsofthehiv1envelopeglycoproteinfusionpeptide AT anitasarkar capturingtheinherentstructuraldynamicsofthehiv1envelopeglycoproteinfusionpeptide AT pavelpugach capturingtheinherentstructuraldynamicsofthehiv1envelopeglycoproteinfusionpeptide AT rogierwsanders capturingtheinherentstructuraldynamicsofthehiv1envelopeglycoproteinfusionpeptide AT johnpmoore capturingtheinherentstructuraldynamicsofthehiv1envelopeglycoproteinfusionpeptide AT andrewbward capturingtheinherentstructuraldynamicsofthehiv1envelopeglycoproteinfusionpeptide AT ianawilson capturingtheinherentstructuraldynamicsofthehiv1envelopeglycoproteinfusionpeptide
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Capturing the inherent structural dynamics of the HIV-1 envelope glycoprotein fusion peptide

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