scholarly journals Oligomeric Structure and Three-Dimensional Fold of the HIV gp41 Membrane-Proximal External Region and Transmembrane Domain in Phospholipid Bilayers

2018 ◽  
Vol 140 (26) ◽  
pp. 8246-8259 ◽  
Author(s):  
Byungsu Kwon ◽  
Myungwoon Lee ◽  
Alan J. Waring ◽  
Mei Hong
Keyword(s):  
Transmembrane Domain ◽  
Three Dimensional ◽  
Phospholipid Bilayers ◽  
Oligomeric Structure ◽  
External Region ◽  
Membrane Proximal External Region ◽  
Hiv Gp41

scholarly journals Structural Characterization of HIV gp41 with the Membrane-proximal External Region

2010 ◽  
Vol 285 (31) ◽  
pp. 24290-24298 ◽  
Author(s):  
Wuxian Shi ◽  
Jen Bohon ◽  
Dong P. Han ◽  
Habtom Habte ◽  
Yali Qin ◽  
...  
Keyword(s):  
Structural Characterization ◽  
External Region ◽  
Membrane Proximal External Region ◽  
Hiv Gp41

scholarly journals Predicted 3D Models of the SARS-CoV-2 Spike Protein Membrane Proximal External Region and Transmembrane Domain

2020 ◽  
Author(s):  
Alexander Izvorski
Keyword(s):  
Large Scale ◽  
Transmembrane Domain ◽  
Energy Landscape ◽  
Transmembrane Helix ◽  
3D Models ◽  
Spike Protein ◽  
Heptad Repeat ◽  
External Region ◽  
Membrane Proximal External Region ◽  
Protein Membrane

The transmembrane helix domain (TMD), membrane proximal external region (MPER) and part of heptad repeat 2 (HR2) domain in SARS-CoV-2 spike protein were modelled using a constrained fold-and-dock strategy. The resulting structures were clustered and their large scale pose variability and energy landscape is described; several representative models are discussed. The results suggest considerable flexibility in the conformation of those regions, which may have an important role in the ability of spike protein to fuse the cell and viral membranes.

scholarly journals Structure of the membrane proximal external region of HIV-1 envelope glycoprotein

2018 ◽  
Vol 115 (38) ◽  
pp. E8892-E8899 ◽  
Author(s):  
Qingshan Fu ◽  
Md Munan Shaik ◽  
Yongfei Cai ◽  
Fadi Ghantous ◽  
Alessandro Piai ◽  
...  
Keyword(s):  
Lipid Bilayer ◽  
Envelope Glycoprotein ◽  
Neutralizing Antibodies ◽  
Transmembrane Domain ◽  
Bilayer Membrane ◽  
Antigenic Analysis ◽  
External Region ◽  
Membrane Proximal External Region ◽  
Electron Cryotomography ◽  
Hiv 1

The membrane-proximal external region (MPER) of the HIV-1 envelope glycoprotein (Env) bears epitopes of broadly neutralizing antibodies (bnAbs) from infected individuals; it is thus a potential vaccine target. We report an NMR structure of the MPER and its adjacent transmembrane domain in bicelles that mimic a lipid-bilayer membrane. The MPER lies largely outside the lipid bilayer. It folds into a threefold cluster, stabilized mainly by conserved hydrophobic residues and potentially by interaction with phospholipid headgroups. Antigenic analysis and comparison with published images from electron cryotomography of HIV-1 Env on the virion surface suggest that the structure may represent a prefusion conformation of the MPER, distinct from the fusion-intermediate state targeted by several well-studied bnAbs. Very slow bnAb binding indicates that infrequent fluctuations of the MPER structure give these antibodies occasional access to alternative conformations of MPER epitopes. Mutations in the MPER not only impede membrane fusion but also influence presentation of bnAb epitopes in other regions. These results suggest strategies for developing MPER-based vaccine candidates.

scholarly journals The Atomic Structure of the HIV-1 gp41 Transmembrane Domain and Its Connection to the Immunogenic Membrane-proximal External Region

2015 ◽  
Vol 290 (21) ◽  
pp. 12999-13015 ◽  
Author(s):  
Beatriz Apellániz ◽  
Edurne Rujas ◽  
Soraya Serrano ◽  
Koldo Morante ◽  
Kouhei Tsumoto ◽  
...  
Keyword(s):  
Atomic Structure ◽  
Transmembrane Domain ◽  
External Region ◽  
Membrane Proximal External Region ◽  
Hiv 1
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