ArticleThe journal of physical chemistry. C, Nanomaterials and interfaces2010
Multiple Proton Confinement in the M2 Channel from the Influenza A Virus.
Article in The journal of physical chemistry. C, Nanomaterials and interfaces, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The trial behind it
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Who cites it
20 citing papers in PubMed, 29 citations in OpenAlex.
- The interplay of polarizable water and protein in the activation of the M2 channel.Frontiers in pharmacology · 2025Article
- From Acid Activation Mechanisms of Proton Conduction to Design of Inhibitors of the M2 Proton Channel of Influenza A Virus.Frontiers in molecular biosciences · 2021Review
- Transport-Relevant Protein Conformational Dynamics and Water Dynamics on Multiple Time Scales in an Archetypal Proton Channel: Insights from Solid-State NMR.Journal of the American Chemical Society · 2018Article
- XFEL structures of the influenza M2 proton channel: Room temperature water networks and insights into proton conduction.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Does Proton Conduction in the Voltage-Gated HThe journal of physical chemistry. B · 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
- High-resolution structures of the M2 channel from influenza A virus reveal dynamic pathways for proton stabilization and transduction.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Hydrogen-bonded water molecules in the M2 channel of the influenza A virus guide the binding preferences of ammonium-based inhibitors.The journal of physical chemistry. B · 2015Article
- Proton release from the histidine-tetrad in the M2 channel of the influenza A virus.The journal of physical chemistry. B · 2014Article
- Multiscale simulation reveals a multifaceted mechanism of proton permeation through the influenza A M2 proton channel.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- 2D IR spectroscopy reveals the role of water in the binding of channel-blocking drugs to the influenza M2 channel.The Journal of chemical physics · 2014Article
- 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
- Proton affinity of the histidine-tryptophan cluster motif from the influenza A virus fromChemical physics · 2013Article
- Article
- Structure and inhibition of the drug-resistant S31N mutant of the M2 ion channel of influenza A virus.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Structural basis for proton conduction and inhibition by the influenza M2 protein.Protein science : a publication of the Protein Society · 2012Review
- Mechanism of function of viral channel proteins and implications for drug development.International review of cell and molecular biology · 2012Review
- Molecular dynamics simulation directed rational design of inhibitors targeting drug-resistant mutants of influenza A virus M2.Journal of the American Chemical Society · 2011Article
- Structural and dynamic mechanisms for the function and inhibition of the M2 proton channel from influenza A virus.Current opinion in structural biology · 2011Review
- Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The tetrameric M2 protein bundle of the influenza A virus is the proton channel responsible for the acidification of the viral interior, a key step in the infection cycle. Selective proton transport is achieved by successive protonation of the conserved histidine amino acids at position 37. A recent X-ray structure of the tetrameric transmembrane (TM) domain of the protein (residues 22-46) resolved several water clusters in the channel lumen, which suggest possible proton pathways to the His37 residues. To explore this hypothesis, we have carried out molecular dynamics (MD) simulations of a proton traveling towards the His37 side chains using MD with classical and quantum force fields. Diffusion through the first half of the channel to the "entry" water cluster near His37 may be hampered by significant kinetic barriers due to electrostatic repulsion. However, once in the entry cluster, a proton can move to one of the acceptor His37 in a nearly barrierless fashion, as evidenced both by MD simulations and a scan of the potential energy surface (PES). Water molecules of the entry cluster, although confined in the M2 pore and restricted in their motions, can conduct protons with a rate very similar to that of bulk water.
Identifiers
What OpenQuestion holds
Registered trials
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.