pH-dependent tetramerization and amantadine binding of the transmembrane helix of M2 from the influenza A virus.

@article{Salom2000pHdependentTA,
  title={pH-dependent tetramerization and amantadine binding of the transmembrane helix of M2 from the influenza A virus.},
  author={David Salom and Brian R. Hill and James D. Lear and William F. DeGrado},
  journal={Biochemistry},
  year={2000},
  volume={39 46},
  pages={
          14160-70
        }
}
The M2 proton channel from the influenza A virus is a small protein with a single transmembrane helix that associates to form a tetramer in vivo. This protein forms proton-selective ion channels, which are the target of the drug amantadine. Here, we propose a mechanism for the pH-dependent association, and amantadine binding of M2, based on studies of a peptide representing the M2 transmembrane segment in dodecylphosphocholine micelles. Using analytical ultracentrifugation, we find that the… CONTINUE READING
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