Elsevier

Virology

Volume 202, Issue 1, July 1994, Pages 287-293
Virology

Regular Article
Neutron Diffraction Reveals the Site of Amantadine Blockade in the Influenza A M2 Ion Channel

https://doi.org/10.1006/viro.1994.1345Get rights and content

Abstract

The influenza A M2 protein forms proton channels which are blocked by the anti-influenza drug amantadine. Using the technique of neutron diffraction with both deuterium-labeled amantadine and influenza A M2 peptides, this study has directly located the position of interaction between the drug and the transmembrane domain of M2. Amantadine is found 0.5 nm from the center of the bilayer in an area between Val 27 and Ser 31, a location consistent with the formation of a steric block within the ion channel. Similar experiments with amantadine and an amantadine-resistant mutant peptide showed no such interaction.

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Cited by (94)

  • Assembly of the M2 Tetramer Is Strongly Modulated by Lipid Chain Length

    2010, Biophysical Journal
    Citation 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).

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