ArticleBiophysical journal2005
A computational study of the closed and open states of the influenza a M2 proton channel.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Molecular biophysics and inhibition mechanism of influenza virus A M2 viroporin by adamantane-based drugs - Challenges in designing antiviral agents.Journal of structural biology: X · 2025Article
- Increased Dissociation of Adamantanamines in Influenza A M2 S31N with Partial Block by Rimantadine.Biophysical journal · 2020Article
- All-atom virus simulations.Current opinion in virology · 2018Review
- Water is an active matrix of life for cell and molecular biology.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Acid activation mechanism of the influenza A M2 proton channel.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Why bound amantadine fails to inhibit proton conductance according to simulations of the drug-resistant influenza A M2 (S31N).The journal of physical chemistry. B · 2015Article
- Activation and proton transport mechanism in influenza A M2 channel.Biophysical journal · 2013Article
- Exploring Histidine Conformations in the M2 Channel Lumen of the Influenza A Virus at Neutral pH via Molecular Simulations.The journal of physical chemistry letters · 2013Article
- Article
- Modeling the membrane environment has implications for membrane protein structure and function: influenza A M2 protein.Protein science : a publication of the Protein Society · 2013Review
- Structural and dynamic mechanisms for the function and inhibition of the M2 proton channel from influenza A virus.Current opinion in structural biology · 2011Review
- pH-driven helix rotations in the influenza M2 H+ channel: a potential gating mechanism.European biophysics journal : EBJ · 2010Article
- Functional studies and modeling of pore-lining residue mutants of the influenza a virus M2 ion channel.Biochemistry · 2010Article
- Structure and dynamics of the influenza A M2 channel: a comparison of three structures.Journal of molecular modeling · 2009Article
- Article
- Structure and function of the influenza A M2 proton channel.Biochemistry · 2009Article
- Equilibrium exchange processes of the aqueous tryptophan dipeptide.The journal of physical chemistry. B · 2009Article
- Computational studies of gramicidin permeation: an entry way sulfonate enhances cation occupancy at entry sites.Biochimica et biophysica acta · 2009Article
- Molecular dynamics calculations suggest a conduction mechanism for the M2 proton channel from influenza A virus.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Self-assembly of a simple membrane protein: coarse-grained molecular dynamics simulations of the influenza M2 channel.Biophysical journal · 2008Article
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2 authors.
Funding
Abstract
In this study, four possible conformations of the His-37 and Trp-41 residues for the closed state of the influenza M2 ion channel were identified by a conformation scan based on a solid-state NMR restraint. In the four conformations, the His-37 residue can be of either the t-160 or t60 rotamer, whereas Trp-41 can be of either the t-105 or t90 rotamer. These conformations were further analyzed by density functional theory calculations and molecular dynamics simulations, and the data indicate that the His-37 residue most likely adopts the t60 rotamer and should be monoprotonated at the delta-nitrogen site, whereas Trp-41 adopts the t90 rotamer. This result is consistent with published experimental data and points to a simple gating mechanism: in the closed state, the His-37 and Trp-41 residues adopt the (t60, t90) conformation, which nearly occludes the pore, preventing nonproton ions from passing through due to the steric and desolvation effects. Moreover, the His-37 tetrad interrupts the otherwise continuous hydrogen-bonding network of the pore water by forcing the water molecules above and below it to adopt opposite orientations, thus adding to the blockage of proton shuttling. The channel can be easily opened by rotating the His-37 chi2 angle from 60 to 0 degrees . This open structure allows pore water to penetrate the constrictive region and to form a continuous water wire for protons to shuttle through, while being still narrow enough to exclude other ions.
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