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.
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Fuchs, S., Neumann, D., Safran, A. (1986). What Can We Learn about the Acetylcholine Receptor from Synthetic Peptides?. In: Maelicke, A. (eds) Nicotinic Acetylcholine Receptor. NATO ASI Series, vol 3. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-71649-2_5
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DOI: https://doi.org/10.1007/978-3-642-71649-2_5
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