Regular ArticleNeutron Diffraction Reveals the Site of Amantadine Blockade in the Influenza A M2 Ion Channel
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Cited by (94)
Mechanism of Function of Viral Channel Proteins and Implications for Drug Development
2012, International Review of Cell and Molecular BiologyDesign and synthesis of bioactive adamantanaminoalcohols and adamantanamines
2010, European Journal of Medicinal ChemistryAssembly of the M2 Tetramer Is Strongly Modulated by Lipid Chain Length
2010, Biophysical JournalCitation Excerpt :The M2 TM domain (residues 22–46) was recently identified as the minimal functional unit of the protein that is capable of assembling into a ligand-activated proton channel (22). Similarly to the full-length protein, the isolated M2 TM helix has the ability to form tetramers, conduct protons, and bind amantadine (22–27). The structure of the tetramer has been determined, revealing a symmetric (or pseudosymmetric), left-handed, parallel tetramer bundle (28–35).
α-Helical transmembrane peptides: A "Divide and Conquer" approach to membrane proteins
2010, Chemistry and Physics of Lipids
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