ArticleBiophysical journal2002
Molecular dynamics investigation of membrane-bound bundles of the channel-forming transmembrane domain of viral protein U from the human immunodeficiency virus HIV-1.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Advances in Viroporin Function and Structure: A Comparative Analysis of Alphavirus 6K with Well-Characterized Viroporins.Viruses · 2025Review
- All-atom virus simulations.Current opinion in virology · 2018Review
- Viral channel forming proteins--How to assemble and depolarize lipid membranes in silico.Biochimica et biophysica acta · 2016Review
- Atomistic detailed mechanism and weak cation-conducting activity of HIV-1 Vpu revealed by free energy calculations.PloS one · 2014Article
- Molecular dynamics simulations reveal the HIV-1 Vpu transmembrane protein to form stable pentamers.PloS one · 2013Article
- Article
- Viroporins: structure and biological functions.Nature reviews. Microbiology · 2012Review
- Mechanism of function of viral channel proteins and implications for drug development.International review of cell and molecular biology · 2012Review
- BST-2 is rapidly down-regulated from the cell surface by the HIV-1 protein Vpu: evidence for a post-ER mechanism of Vpu-action.Virology · 2011Article
- The HIV-1 Vpu viroporin inhibitor BIT225 does not affect Vpu-mediated tetherin antagonism.PloS one · 2011Article
- Modulation of HIV-1-host interaction: role of the Vpu accessory protein.Retrovirology · 2010Review
- Oligomerization state and supramolecular structure of the HIV-1 Vpu protein transmembrane segment in phospholipid bilayers.Protein science : a publication of the Protein Society · 2010Article
- Coarse-grained molecular dynamics of tetrameric transmembrane peptide bundles within a lipid bilayer.Chemistry and physics of lipids · 2010Article
- The Vpu protein: new concepts in virus release and CD4 down-modulation.Current HIV research · 2010Review
- Antiviral activity of the interferon-induced cellular protein BST-2/tetherin.AIDS research and human retroviruses · 2009Review
- Vpu matchmakers as a therapeutic strategy for HIV infection.PLoS pathogens · 2009Article
- Application of solid-state NMR restraint potentials in membrane protein modeling.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2008Article
- Oligomerization of the human immunodeficiency virus type 1 (HIV-1) Vpu protein--a genetic, biochemical and biophysical analysis.Virology journal · 2007Article
- Structure, dynamics and topology of membrane polypeptides by oriented 2H solid-state NMR spectroscopy.European biophysics journal : EBJ · 2007Article
- Structure and dynamics of model pore insertion into a membrane.Biophysical journal · 2005Article
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5 authors.
Funding
Abstract
Molecular dynamics (MD) simulations have been carried out on bundles of the channel-forming transmembrane (TM) domain of the viral protein U (VPU(1-27) and VPU(6-27)) from the human immunodeficiency virus (HIV-1). Simulations of hexameric and pentameric bundles of VPU(6-27) in an octane/water membrane mimetic system suggested that the pentamer is the preferred oligomer. Accordingly, an unconstrained pentameric helix bundle of VPU(1-27) was then placed in a hydrated palmitoyl-oleyl-3-n-glycero-phosphatidylethanolamine (POPE) lipid bilayer and its structural properties calculated from a 3-ns MD run. Some water molecules, initially inside the channel lumen, were expelled halfway through the simulation and the bundle adopted a conical structure reminiscent of previous MD results obtained for VPU(6-27) in an octane/water system. The pore constriction generated may correspond to a closed state of the channel and underlies the relocation of the W residue toward the pore lumen. The relative positions of the helices with respect to the bilayer and their interactions with the lipids are discussed. The observed structure is stabilized via specific interactions between the VPU helices and the carbonyl oxygen atoms of the lipid molecules, particularly at the Q and S residues.
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