Tryptophan substitutions at the lipid-exposed transmembrane segment M4 of Torpedo californica acetylcholine receptor govern channel gating.

Abstract

Our previous amino acid substitutions at the postulated lipid-exposed transmembrane segment M4 of the Torpedo californica acetylcholine receptor (AChR) focused on the alpha C418 position. A tryptophan substitution on the alpha C418 produced a 3-fold increase in normalized macroscopic response to acetylcholine in voltage-clamped Xenopus laevis oocytes (Lee… (More)

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Cite this paper

@article{Lasalde1996TryptophanSA, title={Tryptophan substitutions at the lipid-exposed transmembrane segment M4 of Torpedo californica acetylcholine receptor govern channel gating.}, author={Jos{\'e} A. Lasalde and Shiori Tamamizu and Daniel H. Butler and C R Vibat and B. Hung and Mark G. McNamee}, journal={Biochemistry}, year={1996}, volume={35 45}, pages={14139-48} }