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Molecular characterization of the specificity of interactions of various neurotoxins on two distinct nicotinic acetylcholine receptors.

Abstract : Snake curaremimetic toxins are currently classified as short-chain and long-chain toxins according to their size and their number of disulfide bonds. All these toxins bind with high affinity to muscular-type nicotinic acetylcholine receptor, whereas only long toxins recognize the $\alpha$7 receptor with high affinity. On the basis of binding experiments with Torpedo or neuronal $\alpha$7 receptors using wild-type and mutated neurotoxins, we characterized the molecular determinants involved in these different recognition processes. The functional sites by which long and short toxins interact with the muscular-type receptor include a common core of highly conserved residues and residues that are specific to each of toxin families. Furthermore, the functional sites through which alpha-cobratoxin, a long-chain toxin, interacts with muscular and $\alpha$7 receptors share similarities but also marked differences. Our results reveal that the three-finger fold toxins have evolved toward various specificities by displaying distinct functional sites.
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https://hal-pasteur.archives-ouvertes.fr/pasteur-01719382
Contributor : Ana Cova Rodrigues <>
Submitted on : Wednesday, February 28, 2018 - 11:06:15 AM
Last modification on : Wednesday, October 14, 2020 - 4:10:19 AM

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Denis Servent, Stéphanie Antil-Delbeke, Carole Gaillard, Pierre-Jean Corringer, Jean-Pierre Changeux, et al.. Molecular characterization of the specificity of interactions of various neurotoxins on two distinct nicotinic acetylcholine receptors.. European Journal of Pharmacology, Elsevier, 2000, 393, pp.197-204. ⟨10.1016/S0014-2999(00)00095-9⟩. ⟨pasteur-01719382⟩

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