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

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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Bibliographic Details
Main Authors: Sonu Kumar, Anita Sarkar, Pavel Pugach, Rogier W. Sanders, John P. Moore, Andrew B. Ward, Ian A. Wilson
Format: Article
Language:English
Published: Nature Publishing Group 2019-02-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-019-08738-5
Description
Summary: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.
ISSN:2041-1723

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