Homologous mutations on different subunits cause unequal but additive effects on n-alcohol block in the nicotinic receptor pore.

@article{Forman1997HomologousMO,
  title={Homologous mutations on different subunits cause unequal but additive effects on n-alcohol block in the nicotinic receptor pore.},
  author={Stuart A. Forman},
  journal={Biophysical journal},
  year={1997},
  volume={72 5},
  pages={2170-9}
}
Hydrophobic antagonists of the nicotinic acetylcholine receptor inhibit channel activity by binding within the transmembrane pore formed by the second of four transmembrane domains (M2) on each of the receptor's subunits. Hydrophobic mutagenesis near the middle (10' locus) of the alpha-subunit M2 domain results in channels that are much more sensitive to block by long-chain alcohols and general anesthetics, indicating that the inhibitory site on wild-type receptors is nearby. To determine… CONTINUE READING