Abstract
Most theories of nervous system function depend heavily on the existence and properties of the synapse. For this reason, this structure has been a focal point for neuroscience research for many decades. The best understood synapse is the neuromuscular junction because of its accessibility to biochemical and electrophysiological techniques and because of its elegant, well-defined structure. The nicotinic acetylcholine (ACh) receptor found in the postsynaptic membrane binds ACh released from the nerve. The binding of ACh results in a conformational change in the receptor that opens a channel permeable to cations. The resulting ion flux depolarizes the muscle and ultimately leads to muscle contraction. Thus the ACh receptor contains both a ligand-binding domain as well as a channel domain. Biological and structural studies have shown that the muscle nicotinic ACh receptor is a glycoprotein made up of five subunits with the stoichiometry α2βγδ; each of these subunits has a molecular weight between 40,000 and 60,000, and is encoded by a separate gene. This complex has been shown in reconstitution experiments to be a functional receptor containing both a ligand-binding site and a ligand-gated channel (for recent reviews, see Conti-Tronconi and Raftery, 1982; Popot and Changeux, 1984; Stroud and Finer-Moore, 1985; Karlin et al., 1986; McCarthy et al.,1986).
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Heinemann, S. et al. (1987). Molecular Biology of the Neural and Muscle Nicotinic Acetylcholine Receptors. In: Heinemann, S., Patrick, J. (eds) Molecular Neurobiology. Current Topics in Neurobiology. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-7488-0_3
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