ArticleBiophysical journal2000
Exploring models of the influenza A M2 channel: MD simulations in a phospholipid bilayer.
Article in Biophysical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 97 citations in OpenAlex.
- Water in Nanopores and Biological Channels: A Molecular Simulation Perspective.Chemical reviews · 2020Review
- Decoupled side chain and backbone dynamics for proton translocation - M2 of influenza A.Journal of molecular modeling · 2017Article
- Viral channel forming proteins--How to assemble and depolarize lipid membranes in silico.Biochimica et biophysica acta · 2016Review
- Philosophy of voltage-gated proton channels.Journal of the Royal Society, Interface · 2014Review
- Activation and proton transport mechanism in influenza A M2 channel.Biophysical journal · 2013Article
- Computational modeling of the p7 monomer from HCV and its interaction with small molecule drugs.SpringerPlus · 2013Article
- Viral channel forming proteins - modeling the target.Biochimica et biophysica acta · 2011Review
- Study on phylogenetic relationships, variability, and correlated mutations in M2 proteins of influenza virus A.PloS one · 2011Article
- Ion channels as antivirus targets.Virologica Sinica · 2010Review
- Voltage-gated proton channels find their dream job managing the respiratory burst in phagocytes.Physiology (Bethesda, Md.) · 2010Review
- Molecular dynamics studies of the transmembrane domain of gp41 from HIV-1.Biochimica et biophysica acta · 2009Article
- Article
- Structure and function of the influenza A M2 proton channel.Biochemistry · 2009Article
- Self-assembly of a simple membrane protein: coarse-grained molecular dynamics simulations of the influenza M2 channel.Biophysical journal · 2008Article
- A secondary gate as a mechanism for inhibition of the M2 proton channel by amantadine.The journal of physical chemistry. B · 2008Article
- Application of solid-state NMR restraint potentials in membrane protein modeling.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2008Article
- Molecular dynamics simulation of the Escherichia coli NikR protein: equilibrium conformational fluctuations reveal interdomain allosteric communication pathways.Journal of molecular biology · 2008Article
- Proton transport behavior through the influenza A M2 channel: insights from molecular simulation.Biophysical journal · 2007Article
- Model of a putative pore: the pentameric alpha-helical bundle of SARS coronavirus E protein in lipid bilayers.Biophysical journal · 2006Article
- A computational study of the closed and open states of the influenza a M2 proton channel.Biophysical journal · 2005Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The M2 protein of influenza A virus forms homotetrameric helix bundles, which function as proton-selective channels. The native form of the protein is 97 residues long, although peptides representing the transmembrane section display ion channel activity, which (like the native channel) is blocked by the antiviral drug amantadine. As a small ion channel, M2 may provide useful insights into more complex channel systems. Models of tetrameric bundles of helices containing either 18 or 22 residues have been simulated while embedded in a fully hydrated 1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphatidylcholine bilayer. Several different starting models have been used. These suggest that the simulation results, at least on a nanosecond time scale, are sensitive to the exact starting structure. Electrostatics calculations carried out on a ring of four ionizable aspartate residues at the N-terminal mouth of the channel suggest that at any one time, only one will be in a charged state. Helix bundle models were mostly stable over the duration of the simulation, and their helices remained tilted relative to the bilayer normal. The M2 helix bundles form closed channels that undergo breathing motions, alternating between a tetramer and a dimer-of-dimers structure. Under these conditions either the channel forms a pocket of trapped waters or it contains a column of waters broken predominantly at the C-terminal mouth of the pore. These waters exhibit restricted motion in the pore and are effectively "frozen" in a way similar to those seen in previous simulations of a proton channel formed by a four-helix bundle of a synthetic leucine-serine peptide (, Biophys. J. 77:2400-2410).
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.