ArticleAngewandte Chemie (International ed. in English)2021
Pore-Bound Water at the Key Residue Histidine 37 in Influenza A M2.
Article in Angewandte Chemie (International ed. in English), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Structural Transition from Closed to Open for the Influenza A M2 Proton Channel as Observed by Proton-Detected Solid-State NMR.Journal of the American Chemical Society · 2025Article
- Solid state NMR spectral editing of histidine, arginine and lysine using Hadamard encoding.Journal of biomolecular NMR · 2025Article
- Review
- Real-time tracking of drug binding to influenza A M2 reveals a high energy barrier.Journal of structural biology: X · 2023Article
- Review
- YWHAG inhibits influenza a virus replication by suppressing the release of viral M2 protein.Frontiers in microbiology · 2022Article
- Pore-Bound Water at the Key Residue Histidine 37 in Influenza A M2.Angewandte Chemie (International ed. in English) · 2021Article
- 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
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Atomic details of structured water molecules are indispensable to understand the thermodynamics of important biological processes including the proton conduction mechanism of the M2 protein. Despite the expectation of structured water molecules based on crystal structures of Influenza A M2, only two water populations have been observed by NMR in reconstituted lipid bilayer samples. These are the bulk- and lipid-associated water populations typically seen in membrane samples. Here, we detect a bound water molecule at a chemical shift of 11 ppm, located near the functional histidine 37 residue in the M2 conductance domain, which comprises residues 18 to 60. Combining 100 kHz magic-angle spinning NMR, dynamic nuclear polarization and density functional theory calculations, we show that the bound water forms a hydrogen bond to the δ1 nitrogen of histidine 37.
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