Brain α-Neurotoxin-Binding Proteins and Nicotinic Acetylcholine Receptors
The study of the nicotinic acetylcholine receptor (AChR) of skeletal muscle and fish electric organ has been greatly facilitated by the application of the α-neurotoxins (postsynaptic toxins) of elapid and hydrophid snake venoms, such as α-bungarotoxin (α-BTX), introduced by C. Y. Lee (Lee, 1973). These polypeptide toxins bind to the receptor with KD values 10−9 and 10−12 M, causing blockade of function. It has been found that the peripheral (vertebrate muscle and electric organ) type of AChR invariably has two of these high-affinity α-toxin binding sites, one on each of the α subunits of its α2βγδ pentameric structure (for reviews see Dolly and Barnard, 1984; Popot and Changeux, 1984) . However, attempts to use α-bungarotoxin as a probe for the more poorly-characterised, neuronal nicotinic receptors have caused a great deal of confusion.
KeywordsTyrosine Nicotine Cysteine Polypeptide Acetylcholine
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