Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Molecular surface of tarantula toxins interacting with voltage sensors in K(v) channels.

The Journal of general physiology - 1 Apr 2004

Wang Julia M, Roh Soung Hun, Kim Sunghwan, Lee Chul Won, Kim Jae Il, Swartz Kenton J

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Circular Dichroism

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Ion Channel Gating

Share to Oocytes

Share to Potassium Channels, Voltage-Gated

Share to Protein Binding

Share to Protein Structure, Tertiary

Share to Xenopus

Source

Open in PubMed Open full text

Identifiers

PMID: 15051809
DOI: 10.1085/jgp.200309005
PMCID: PMC2217462

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Molecular surface of tarantula toxins interacting with voltage sensors in K(v) channels.PMID 15051809Read ↗

Structure and function of the voltage sensor of sodium channels probed by a beta-scorpion toxin.Semantic proximity Read ↗

Analysis of the interaction of tarantula toxin Jingzhaotoxin-III (β-TRTX-Cj1α) with the voltage sensor of Kv2.1 uncovers the molecular basis for cross-activities on Kv2.1 and Nav1.5 channels.Semantic proximity Read ↗

Molecular surface of JZTX-V (β-Theraphotoxin-Cj2a) interacting with voltage-gated sodium channel subtype NaV1.4.Semantic proximity Read ↗

Scanning mutagenesis of a Janus-faced atracotoxin reveals a bipartite surface patch that is essential for neurotoxic function.Semantic proximity Read ↗

Active Sites of Spinoxin, a Potassium Channel Scorpion Toxin, Elucidated by Systematic Alanine Scanning.Semantic proximity Read ↗

Palmitoylation influences the function and pharmacology of sodium channels.Semantic proximity Read ↗

Interaction between extracellular Hanatoxin and the resting conformation of the voltage-sensor paddle in Kv channels.Semantic proximity Read ↗

Mapping the receptor site for hanatoxin, a gating modifier of voltage-dependent K+ channels.Semantic proximity Read ↗

Molecular basis of the tarantula toxin jingzhaotoxin-III (β-TRTX-Cj1α) interacting with voltage sensors in sodium channel subtype Nav1.5.Semantic proximity Read ↗

Evidence for multiple effects of ProTxII on activation gating in Na(V)1.5.Semantic proximity Read ↗

Targeting the voltage sensor of Kv7.2 voltage-gated K+ channels with a new gating-modifier.Semantic proximity Read ↗

Voltage sensor-trapping: enhanced activation of sodium channels by beta-scorpion toxin bound to the S3-S4 loop in domain II.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.