The conformation of the pore region of the M2 proton channel depends on lipid bilayer environment.

@article{DuongLy2005TheCO,
  title={The conformation of the pore region of the M2 proton channel depends on lipid bilayer environment.},
  author={Krisna C Duong-Ly and Vikas Nanda and William F. DeGrado and Kathleen P Howard},
  journal={Protein science : a publication of the Protein Society},
  year={2005},
  volume={14 4},
  pages={856-61}
}
The M2 protein from influenza A virus is a 97-amino-acid protein with a single transmembrane helix that forms proton-selective channels essential to virus function. The hydrophobic transmembrane domain of the M2 protein (M2TM) contains a sequence motif that mediates the formation of functional tetramers in membrane environments. A variety of structural models have previously been proposed which differ in the degree of helix tilt, with proposed tilts ranging from approximately 15 degrees to 38… CONTINUE READING

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