Subunit organization and structure of an acetylcholine receptor.

Robert H Fairclough, J. Finer-Moore, R. A. Love, D. Kristofferson, P. J. Desmeules, R. M. Stroud

Research output: Contribution to journalArticle

45 Scopus citations

Abstract

We have learned the positions of the alpha-subunits around the AChR rosette and the location of the toxin on the synaptic crest. A charge/hydrophobic character map of the 40 A X 30 A receptor surface that binds alpha-bungarotoxin has been constructed. A beta-structure domain surrounds the agonist binding site on the alpha-subunits, as predicted by amphipathic Fourier sequence analysis. The ion channel may be constructed from five amphipathic helices, which insert into the bilayer as the alpha2 beta gamma delta subunits come together. They form a water-filled channel on one side and interface with hydrophobic helices in each subunit on the other.

Original languageEnglish (US)
Pages (from-to)9-20
Number of pages12
JournalCold Spring Harbor Symposia on Quantitative Biology
Volume48 Pt 1
StatePublished - 1983
Externally publishedYes

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Molecular Biology

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  • Cite this

    Fairclough, R. H., Finer-Moore, J., Love, R. A., Kristofferson, D., Desmeules, P. J., & Stroud, R. M. (1983). Subunit organization and structure of an acetylcholine receptor. Cold Spring Harbor Symposia on Quantitative Biology, 48 Pt 1, 9-20.