Abstract
Snakes produce a diversity of toxins, the α-neurotoxins or curaremimetic toxins, which act on nicotinic acetylcholine receptors (AChRs). As shown in Table 1, these toxins can be divided into four categories. First, there are the a-neurotoxins, which bind with high affinity to muscular AChRs only. These include a large family of short-chain, three-fingered toxins from Elapidae (elapids and hydrophiids), and the waglerins from Viperidae (Trimeresurus wagleri) (1–3). Second, there are the α/k neurotoxins, which bind with high affinities to both muscular and some neuronal receptors (α7, α8, and α9) (4–6). These toxins correspond to the family of long-chain, three-finger toxins found in venoms from Elapidae, which, until recently (7), were systematically associated with the family of short-chain three-fingered toxins (1). Third, there are the K-neurotoxins, which bind with high affinity to neuronal receptors only. So far, only four toxins of this category have been described and all of them are long-chain, three-fingered toxins from elapid snakes (8,9). Fourth, there are nonconventional neurotoxins with an additional disulfide bond in the first loop. These toxins, also called weak neurotoxins, interact with low affinities (their Kds are in the µM range) on muscular-type AChRs (9a, 9b, 9c, 9d).
Published Version
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