ReviewProtein science : a publication of the Protein Society2013
Modeling the membrane environment has implications for membrane protein structure and function: influenza A M2 protein.
Review in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- Adamantane-based inhibitors of the influenza A M2 proton channel: structure-based design, biological evaluation, and synthetic approaches.RSC medicinal chemistry · 2026Review
- Hemagglutinin and neuraminidase of a non-pathogenic H7N7 avian influenza virus coevolved during the acquisition of intranasal pathogenicity in chickens.Archives of virology · 2024Article
- Cooperativity in regulation of membrane protein function: phenomenological analysis of the effects of pH and phospholipids.Biophysical reviews · 2023Review
- Conformation of influenza AM2 membrane protein in nanodiscs and liposomes.Biochimica et biophysica acta. Biomembranes · 2023Article
- Review
- Influenza AM2 Channel Oligomerization Is Sensitive to Its Chemical Environment.Analytical chemistry · 2021Article
- Put a cork in it: Plugging the M2 viral ion channel to sink influenza.Antiviral research · 2020Review
- M2 amphipathic helices facilitate pH-dependent conformational transition in influenza A virus.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Chirality-Dependent Adsorption between Amphipathic Peptide and POPC Membrane.International journal of molecular sciences · 2019Article
- Structural Analysis and Dynamic Processes of the Transmembrane Segment Inside Different Micellar Environments-Implications for the TM4 Fragment of the Bilitranslocase Protein.International journal of molecular sciences · 2019Article
- The L46P mutant confers a novel allosteric mechanism of resistance toward the influenza A virus M2 S31N proton channel blockers.Molecular pharmacology · 2019Article
- Proton-Induced Conformational and Hydration Dynamics in the Influenza A M2 Channel.Journal of the American Chemical Society · 2019Article
- Binding of a small molecule water channel inhibitor to aquaporin Z examined by solid-state MAS NMR.Journal of biomolecular NMR · 2018Article
- Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.Chemical reviews · 2018Review
- Comparison of NMR and crystal structures of membrane proteins and computational refinement to improve model quality.Proteins · 2018Article
- Influenza A Virus M2 Protein: Roles from Ingress to Egress.International journal of molecular sciences · 2017Review
- Probing Residue-Specific Water-Protein Interactions in Oriented Lipid Membranes via Solid-State NMR Spectroscopy.The journal of physical chemistry. B · 2016Article
- Targeting the Channel Activity of Viroporins.Advances in protein chemistry and structural biology · 2016Review
- The styrene-maleic acid copolymer: a versatile tool in membrane research.European biophysics journal : EBJ · 2016Review
- Dynamic Short Hydrogen Bonds in Histidine Tetrad of Full-Length M2 Proton Channel Reveal Tetrameric Structural Heterogeneity and Functional Mechanism.Structure (London, England : 1993) · 2015Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The M2 protein, a proton channel, from Influenza A has been structurally characterized by X-ray diffraction and by solution and solid-state NMR spectroscopy in a variety of membrane mimetic environments. These structures show substantial backbone differences even though they all present a left-handed tetrameric helical bundle for the transmembrane domain. Variations in the helix tilt influence drug binding and the chemistry of the histidine tetrad responsible for acid activation, proton selectivity and transport. Some of the major structural differences do not arise from the lack of precision, but instead can be traced to the influences of the membrane mimetic environments. The structure in lipid bilayers displays unique chemistry for the histidine tetrad, which binds two protons cooperatively to form a pair of imidazole-imidazolium dimers. The resulting interhistidine hydrogen bonds contribute to a three orders of magnitude enhancement in tetramer stability. Integration with computation has provided detailed understanding of the functional mechanism for proton selectivity, conductance and gating of this important drug target.
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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.