What Can We Learn about the Acetylcholine Receptor from Synthetic Peptides?

  • Sara Fuchs
  • Drorit Neumann
  • Anat Safran
Part of the NATO ASI Series book series (volume 3)

Abstract

The nicotinic acetylcholine receptor (AChR) is a well characterized neurotransmitter receptor and transmembrane ionic channel. It is composed of five subunits in a stoichiometry of α2ßγδ (for reviews see 1–3). The AChR from electric fish has been isolated and the amino acid sequence of the subunits have been deduced by recombinant DNA technology (4–8). The strong homology between the Torpedo AChR and AChR from skeletal muscle of other species made it possible to clone and deduce the sequence of the receptor from muscle tissue, where its amount is 3–4 orders of magnitude lower than that of the Torpedo electric organ (9–13). The sequence data have been the basis for predictions concerning the transmembrane orientation of the AChR subunits, as well as the possible location of the acetylcholine binding site, the glycosylation and phosphorylation sites, and the main immunogenic determinants.

Keywords

Tyrosine Cysteine Serine Polypeptide Resi 

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Copyright information

© Springer-Verlag Berlin Heidelberg 1986

Authors and Affiliations

  • Sara Fuchs
    • 1
  • Drorit Neumann
    • 1
  • Anat Safran
    • 1
  1. 1.Department of Chemical ImmunologyThe Weizmann Institute of ScienceRehovotIsrael

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