ArticleProtein science : a publication of the Protein Society2016
Crystal structure of the drug-resistant S31N influenza M2 proton channel.
Article in Protein science : a publication of the Protein Society, 2016. 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.
- Development of an ultrahigh affinity, trimeric ACE2 biologic as a universal SARS-CoV-2 antagonist.Communications biology · 2025Article
- Influenza A virus resistance to 4'-fluorouridine coincides with viral attenuation in vitro and in vivo.PLoS pathogens · 2024Article
- Real-time tracking of drug binding to influenza A M2 reveals a high energy barrier.Journal of structural biology: X · 2023Article
- The M2 proteins of bat influenza A viruses reveal atypical features compared to conventional M2 proteins.Journal of virology · 2023Article
- Spiers Memorial Lecture: Analysis andFaraday discussions · 2021Article
- Influenza AM2 Channel Oligomerization Is Sensitive to Its Chemical Environment.Analytical chemistry · 2021Article
- Rimantadine Binds to and Inhibits the Influenza A M2 Proton Channel without Enantiomeric Specificity.Biochemistry · 2021Article
- Understanding the Impact of Resistance to Influenza Antivirals.Clinical microbiology reviews · 2021Review
- 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
- Site-directed M2 proton channel inhibitors enable synergistic combination therapy for rimantadine-resistant pandemic influenza.PLoS pathogens · 2020Article
- Put a cork in it: Plugging the M2 viral ion channel to sink influenza.Antiviral research · 2020Review
- Article
- X-ray Crystal Structure of the Influenza A M2 Proton Channel S31N Mutant in Two Conformational States: An Open and Shut Case.Journal of the American Chemical Society · 2019Article
- Viroporins in the Influenza Virus.Cells · 2019Review
- Inhibitors of the M2 Proton Channel Engage and Disrupt Transmembrane Networks of Hydrogen-Bonded Waters.Journal of the American Chemical Society · 2018Article
- Optimization of Detergent-Mediated Reconstitution of Influenza A M2 Protein into Proteoliposomes.Membranes · 2018Article
- Article
- 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
- Binding and Proton Blockage by Amantadine Variants of the Influenza M2Journal of medicinal chemistry · 2017Article
- Expeditious Lead Optimization of Isoxazole-Containing Influenza A Virus M2-S31N Inhibitors Using the Suzuki-Miyaura Cross-Coupling Reaction.Journal of medicinal chemistry · 2017Article
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2 authors.
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Abstract
The M2 protein is a small proton channel found in the influenza A virus that is necessary for viral replication. The M2 channel is the target of a class of drugs called the adamantanes, which block the channel pore and prevent the virus from replicating. In recent decades mutations have arisen in M2 that prevent the adamantanes from binding to the channel pore, with the most prevalent of these mutations being S31N. Here we report the first crystal structure of the S31N mutant crystallized using lipidic cubic phase crystallization techniques and solved to 1.59 Å resolution. The Asn31 residues point directly into the center of the channel pore and form a hydrogen-bonded network that disrupts the drug-binding site. Ordered waters in the channel pore form a continuous hydrogen bonding network from Gly34 to His37.
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