Molecular Structure of the Nicotinic Acetylcholine Receptor
This extract was created in the absence of an abstract.
Excerpt
The nicotinic acetylcholine receptor (AChR) is a postsynaptic membrane protein complex that alters the ion permeability of the membrane as a consequence of binding acetylcholine (ACh) (for review, see Karlin 1980; Changeux 1981; Conti-Tronconi and Raftery 1982). The AChR from the electroplax of the ray Torpedo californica is composed of five subunits present in a molar stoichiometry of α2βγδ (Reynolds and Karlin 1978; Lindstrom et al. 1979; Raftery et al. 1980). The pentameric protein complex is responsible for the binding of agonists, cholinergic antagonists, α-toxins, histrionicotoxin, and local anesthetics as well as for cation translocation (for review, see Karlin 1980; Changeux 1981; Conti-Tronconi and Raftery 1982). A prerequisite to the understanding of the molecular basis for these various functions is to elucidate the primary structures of the constituent polypeptides of the AChR. The aminoterminal 54–56 amino acids of all four polypeptides derived from T. californica have been sequenced (Raftery et...
