Role of a key cysteine residue in the gating of the acetylcholine receptor.


Journal Article

We have examined changes in single-channel behavior that result from conservative amino acid substitutions at the Cys230 residue in the putative first transmembrane region (M1) of the murine nicotinic acetylcholine receptor. Mutations made in the gamma subunit altered the energy barrier for a single closing rate constant in proportion to the size of the substituted side chain. One of these substitutions, when made in the alpha subunits, had no effect on gating. No mutations altered permeation. We conclude that the region surrounding the M1 Cys is involved in the gating of the nicotinic acetylcholine receptor and that the gamma subunit contributes significantly to the control of channel closure.

Full Text

Cited Authors

  • Lo, DC; Pinkham, JL; Stevens, CF

Published Date

  • January 1, 1991

Published In

Volume / Issue

  • 6 / 1

Start / End Page

  • 31 - 40

PubMed ID

  • 1986773

Pubmed Central ID

  • 1986773

Electronic International Standard Serial Number (EISSN)

  • 1097-4199

International Standard Serial Number (ISSN)

  • 0896-6273

Digital Object Identifier (DOI)

  • 10.1016/0896-6273(91)90119-k


  • eng