Abstract
The long α-neurotoxin, α-Bungarotoxin (Bgtx), from the venom of the Taiwan banded krait, Bungarus multicinctus, is a high affinity competitive antagonist of skeletal muscle-type nicotinic acetylcholine receptors (nAChRs) and of certain homo-oligomeric neuronal nicotinic acetylcholine receptors. Bgtx has a long and illustrious record as a valuable tool for the identification, purification, and localization of skeletal muscle-type nAChRs. The structure and function of Bgtx is of special interest as Bgtx is the prototypical member of a large family of curaremimetic α-neurotoxins from the venoms of Elapidae and Hydrophidae snakes. Bgtx has been the focus of extensive studies aimed at discerning the structural basis for its high affinity interaction with nAChRs. Over the past year, our understanding has advanced significantly with the crystal structure of the acetylcholine-binding protein, AChBP, a nAChR extracellular domain homologue, and with structure determinations of Bgtx and its complexes with receptor-s...
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