Cu(II) Inhibition of the Proton Translocation Machinery of the Influenza A Virus M2 Protein*

@article{Gandhi1999CuIIIO,
  title={Cu(II) Inhibition of the Proton Translocation Machinery of the Influenza A Virus M2 Protein*},
  author={Chris S. Gandhi and K Shuck and James Lear and Gregg R. Dieckmann and William F. DeGrado and Robert A. Lamb and Lawrence H. Pinto},
  journal={The Journal of Biological Chemistry},
  year={1999},
  volume={274},
  pages={5474 - 5482}
}
  • Chris S. Gandhi, K Shuck, +4 authors Lawrence H. Pinto
  • Published 1999
  • Chemistry, Medicine
  • The Journal of Biological Chemistry
  • The homotetrameric M2 integral membrane protein of influenza virus forms a proton-selective ion channel. An essential histidine residue (His-37) in the M2 transmembrane domain is believed to play an important role in the conduction mechanism of this channel. Also, this residue is believed to form hydrogen-bonded interactions with the ammonium group of the anti-viral compound, amantadine. A molecular model of this channel suggests that the imidazole side chains of His-37 from symmetry-related… CONTINUE READING

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