ArticleThe Journal of biological chemistry2011
Elucidation of the molecular basis of selective recognition uncovers the interaction site for the core domain of scorpion alpha-toxins on sodium channels.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 45 citations in OpenAlex.
- Allosteric interactions among voltage-sensor modules of sodium channels probed by scorpion toxin modifiers.Journal of neurobiology and physiology · 2022Article
- The Pharmacological and Structural Basis of the AahII-NaFrontiers in pharmacology · 2022Article
- Charge substitutions at the voltage-sensing module of domain III enhance actions of site-3 and site-4 toxins on an insect sodium channel.Insect biochemistry and molecular biology · 2021Article
- Interactions of Sea Anemone Toxins with Insect Sodium Channel-Insights from Electrophysiology and Molecular Docking Studies.Molecules (Basel, Switzerland) · 2021Article
- Structure-Activity Relationship Evaluation of Wasp Toxin β-PMTX Leads to Analogs with Superior Activity for Human Neuronal Sodium Channels.ACS medicinal chemistry letters · 2020Article
- Article
- Two distinct voltage-sensing domains control voltage sensitivity and kinetics of current activation in CaV1.1 calcium channels.The Journal of general physiology · 2016Article
- The hitchhiker's guide to the voltage-gated sodium channel galaxy.The Journal of general physiology · 2016Review
- Review
- Target-Driven Evolution of Scorpion Toxins.Scientific reports · 2015Article
- A surface plasmon resonance approach to monitor toxin interactions with an isolated voltage-gated sodium channel paddle motif.The Journal of general physiology · 2015Article
- Exposure to 50 Hz electromagnetic field changes the efficiency of the scorpion alpha toxin.The journal of venomous animals and toxins including tropical diseases · 2015Article
- Article
- Allosteric interactions between receptor site 3 and 4 of voltage-gated sodium channels: a novel perspective for the underlying mechanism of scorpion sting-induced pain.The journal of venomous animals and toxins including tropical diseases · 2015Article
- Wheat germ in vitro translation to produce one of the most toxic sodium channel specific toxins.Bioscience reports · 2014Article
- Molecular biology of insect sodium channels and pyrethroid resistance.Insect biochemistry and molecular biology · 2014Article
- Sequence variations at I260 and A1731 contribute to persistent currents in Drosophila sodium channels.Neuroscience · 2014Article
- Article
- The insecticidal potential of venom peptides.Cellular and molecular life sciences : CMLS · 2013Review
- Modular organization of α-toxins from scorpion venom mirrors domain structure of their targets, sodium channels.The Journal of biological chemistry · 2013Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Neurotoxin receptor site-3 at voltage-gated Na(+) channels is recognized by various peptide toxin inhibitors of channel inactivation. Despite extensive studies of the effects of these toxins, their mode of interaction with the channel remained to be described at the molecular level. To identify channel constituents that interact with the toxins, we exploited the opposing preferences of LqhαIT and Lqh2 scorpion α-toxins for insect and mammalian brain Na(+) channels. Construction of the DIV/S1-S2, DIV/S3-S4, DI/S5-SS1, and DI/SS2-S6 external loops of the rat brain rNa(v)1.2a channel (highly sensitive to Lqh2) in the background of the Drosophila DmNa(v)1 channel (highly sensitive to LqhαIT), and examination of toxin activity on the channel chimera expressed in Xenopus oocytes revealed a substantial decrease in LqhαIT effect, whereas Lqh2 was as effective as at rNa(v)1.2a. Further substitutions of individual loops and specific residues followed by examination of gain or loss in Lqh2 and LqhαIT activities highlighted the importance of DI/S5-S6 (pore module) and the C-terminal region of DIV/S3 (gating module) of rNa(v)1.2a for Lqh2 action and selectivity. In contrast, a single substitution of Glu-1613 to Asp at DIV/S3-S4 converted rNa(v)1.2a to high sensitivity toward LqhαIT. Comparison of depolarization-driven dissociation of Lqh2 and mutant derivatives off their binding site at rNa(v)1.2a mutant channels has suggested that the toxin core domain interacts with the gating module of DIV. These results constitute the first step in better understanding of the way scorpion α-toxins interact with voltage-gated Na(+)-channels at the molecular level.
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