Nav channel binder containing a specific conjugation-site based on a low toxicity β-scorpion toxin
نویسندگان
چکیده
منابع مشابه
Scorpion β-toxin interference with NaV channel voltage sensor gives rise to excitatory and depressant modes
Scorpion β toxins, peptides of ∼70 residues, specifically target voltage-gated sodium (Na(V)) channels to cause use-dependent subthreshold channel openings via a voltage-sensor trapping mechanism. This excitatory action is often overlaid by a not yet understood depressant mode in which Na(V) channel activity is inhibited. Here, we analyzed these two modes of gating modification by β-toxin Tz1 f...
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Scorpion venom is rich in proteinaceous toxins that affect excitability by impeding ion channel gating. Channel blockers interact with the external region of the pore and obstruct ion conductance, whereas channel modifiers interact with the voltage sensor module hindering the activation or inactivation processes [1-3]. Scorpion toxin modifiers of voltage-gated sodium channels (Navs) are divided...
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The structure of a complex containing a toxin bound to a potassium ion channel has been solved for the first time, revealing how scorpions have designed toxins that can recognize and target the filter that controls the movement of potassium ions through these channels.
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Several naturally occurring polypeptide neurotoxins target specific sites on the voltage-gated sodium channels. Of these, the gating modifier toxins alter the behavior of the sodium channels by stabilizing transient intermediate states in the channel gating pathway. Here we have used an integrated approach that combines electrophysiological and spectroscopic measurements to determine the struct...
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ژورنال
عنوان ژورنال: Scientific Reports
سال: 2017
ISSN: 2045-2322
DOI: 10.1038/s41598-017-16426-x