ArticleBiochimica et biophysica acta2009
Molecular dynamics studies of the transmembrane domain of gp41 from HIV-1.
Article in Biochimica et biophysica acta, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 34 citations in OpenAlex.
- Article
- An engineered HIV-1 Gag-based VLP displaying high antigen density induces strong antibody-dependent functional immune responses.NPJ vaccines · 2023Article
- Structural and functional stability of the sulfur-free surfactant protein B peptide mimic B-YL in synthetic surfactant lipids.BMC pulmonary medicine · 2021Article
- Structure, membrane topology and influence of cholesterol of the membrane proximal region: transmembrane helical anchor sequence of gp41 from HIV.Scientific reports · 2020Article
- The Vaccinia virion: Filling the gap between atomic and ultrastructure.PLoS pathogens · 2019Article
- All-atom virus simulations.Current opinion in virology · 2018Review
- HIV-1 Env gp41 Transmembrane Domain Dynamics Are Modulated by Lipid, Water, and Ion Interactions.Biophysical journal · 2018Article
- Conformation and Trimer Association of the Transmembrane Domain of the Parainfluenza Virus Fusion Protein in Lipid Bilayers from Solid-State NMR: Insights into the Sequence Determinants of Trimer Structure and Fusion Activity.Journal of molecular biology · 2018Article
- The conformational feasibility for the formation of reaching dimer in ASV and HIV integrase: a molecular dynamics study.Journal of biomolecular structure & dynamics · 2017Article
- Hendra virus fusion protein transmembrane domain contributes to pre-fusion protein stability.The Journal of biological chemistry · 2017Article
- Screening for transmembrane association in divisome proteins using TOXGREEN, a high-throughput variant of the TOXCAT assay.Biochimica et biophysica acta · 2016Article
- The Atomic Structure of the HIV-1 gp41 Transmembrane Domain and Its Connection to the Immunogenic Membrane-proximal External Region.The Journal of biological chemistry · 2015Article
- Structural dynamics of native and V260E mutant C-terminal domain of HIV-1 integrase.Journal of computer-aided molecular design · 2015Article
- Complete dissociation of the HIV-1 gp41 ectodomain and membrane proximal regions upon phospholipid binding.Journal of biomolecular NMR · 2015Article
- The dynamics of interconverting D- and E-forms of the HIV-1 integrase N-terminal domain.European biophysics journal : EBJ · 2014Article
- C-terminal tail of human immunodeficiency virus gp41: functionally rich and structurally enigmatic.The Journal of general virology · 2013Review
- Computer-Aided Approaches for Targeting HIVgp41.Biology · 2012Article
- HIV-1 gp41 transmembrane domain interacts with the fusion peptide: implication in lipid mixing and inhibition of virus-cell fusion.Biochemistry · 2012Article
- Neutralizing epitopes in the membrane-proximal external region of HIV-1 gp41 are influenced by the transmembrane domain and the plasma membrane.Journal of virology · 2012Article
- Highly conserved structural properties of the C-terminal tail of HIV-1 gp41 protein despite substantial sequence variation among diverse clades: implications for functions in viral replication.The Journal of biological chemistry · 2011Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Helix-helix interactions in the putative three-helix bundle formation of the gp41 transmembrane (TM) domain may contribute to the process of virus-cell membrane fusion in HIV-1 infection. In this study, molecular dynamics is used to analyze and compare the conformations of monomeric and trimeric forms of the TM domain in various solvent systems over the course of 4 to 23-ns simulations. The trimeric bundles of the TM domain were stable as helices and remained associated in a hydrated POPE lipid bilayer for the duration of the 23-ns simulation. Several stable inter-chain hydrogen bonds, mostly among the three deprotonated arginine residues located at the center of each of the three TM domains, formed in a right-handed bundle embedded in the lipid bilayer. No such bonds were observed when the bundle was left-handed or when the central arginine residue in each of the three TM helices was replaced with isoleucine (R_I mutant), suggesting that the central arginine residues may play an essential role in maintaining the integrity of the three-helix bundle. These observations suggest that formation of the three-helix bundle of the TM domain may play a role in the trimerization of gp41, thought to occur during the virus-cell membrane fusion process.
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