ArticleThe Journal of general physiology2004
Molecular surface of tarantula toxins interacting with voltage sensors in K(v) channels.
Article in The Journal of general physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 101 citations in OpenAlex.
- Alanine Mutagenesis Identifies Specific Amino Acids of Nemertide Alpha-1 Activity and Its Binding to Target Receptors.Journal of natural products · 2026Article
- Spider venom peptides with unique fold selectively block Shaker-type potassium channels.Cellular and molecular life sciences : CMLS · 2025Article
- Article
- Cryo-EM structures of Kv1.2 potassium channels, conducting and non-conducting.bioRxiv : the preprint server for biology · 2024Article
- Dissecting the contributions of membrane affinity and bivalency of the spider venom protein DkTx to its sustained mode of TRPV1 activation.The Journal of biological chemistry · 2023Article
- Chemical Synthesis and NMR Solution Structure of Conotoxin GXIA fromMarine drugs · 2021Article
- Mechanism of hERG inhibition by gating-modifier toxin, APETx1, deduced by functional characterization.BMC molecular and cell biology · 2021Article
- The Tarantula Venom Peptide Eo1a Binds to the Domain II S3-S4 Extracellular Loop of Voltage-Gated Sodium Channel NaFrontiers in pharmacology · 2021Article
- Peptide Toxins Targeting KV Channels.Handbook of experimental pharmacology · 2021Review
- Mapping the Molecular Surface of the Analgesic NaACS pharmacology & translational science · 2020Article
- Spider Knottin Pharmacology at Voltage-Gated Sodium Channels and Their Potential to Modulate Pain Pathways.Toxins · 2019Review
- Kalium 2.0, a comprehensive database of polypeptide ligands of potassium channels.Scientific data · 2019Article
- The tarantula toxin GxTx detains KThe Journal of general physiology · 2019Article
- JZTX-V Targets the Voltage Sensor in Kv4.2 to Inhibit IFrontiers in pharmacology · 2019Article
- Gating modifier toxins isolated from spider venom: Modulation of voltage-gated sodium channels and the role of lipid membranes.The Journal of biological chemistry · 2018Article
- APETx4, a Novel Sea Anemone Toxin and a Modulator of the Cancer-Relevant Potassium Channel KMarine drugs · 2017Article
- Modulatory features of the novel spider toxin μ-TRTX-Df1a isolated from the venom of the spider Davus fasciatus.British journal of pharmacology · 2017Article
- GsMTx4: Mechanism of Inhibiting Mechanosensitive Ion Channels.Biophysical journal · 2017Article
- Molecular Interactions between Tarantula Toxins and Low-Voltage-Activated Calcium Channels.Scientific reports · 2016Article
- Review
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
The venom from spiders, scorpions, and sea anemone contain a rich diversity of protein toxins that interact with ion channel voltage sensors. Although atomic structures have been solved for many of these toxins, the surfaces that are critical for interacting with voltage sensors are poorly defined. Hanatoxin and SGTx are tarantula toxins that inhibit activation of K(v) channels by interacting with each of the four voltage sensors. In this study we set out to identify the active surface of these toxins by alanine-scanning SGTx and characterizing the interaction of each mutant with the K(v)2.1 channel. Examination of the concentration dependence for inhibition identified 15 mutants with little effect on the concentration dependence for toxin inhibition of the K(v)2.1 channel, and 11 mutants that display moderate to dramatic perturbations. Mapping of these results onto the structure of SGTx identifies one face of the toxin where mutations with pronounced perturbations cluster together, and a backside of the toxin where mutations are well tolerated. The active surface of SGTx contains a ring-like assembly of highly polar residues, with two basic residues that are particularly critical, concentrically arranged around a hydrophobic protrusion containing critical aliphatic and aromatic residues. These results identify the active surface of the toxin and reveal the types of side chains that are important for interacting with voltage sensors.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.