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

Mapping the receptor site for alpha-scorpion toxins on a Na+ channel voltage sensor.

Proceedings of the National Academy of Sciences of the United States of America - 13 Sept 2011

Wang Jinti, Yarov-Yarovoy Vladimir, Kahn Roy, Gordon Dalia, Gurevitz Michael, Scheuer Todd, Catterall William A

Abstract excerpt

The α-scorpions toxins bind to the resting state of Na(+) channels and inhibit fast inactivation by interaction with a receptor site formed by domains I and IV. Mutants T1560A, F1610A, and E1613A in domain IV had lower affinities for Leiurus quinquestriatus hebraeus toxin II (LqhII), and mutant E1613R had ~73-fold lower affinity. Toxin dissociation was accelerated by depolarization and increased by these...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acids
Share to Ion Channel Gating

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

Share to Kinetics

Share to Protein Structure, Tertiary

Share to Receptors, Cell Surface

Share to Recombinant Proteins

Share to Scorpion Venoms

Share to Sodium Channels

Source

Open in PubMed Open full text

Identifiers

PMID: 21876146
DOI: 10.1073/pnas.1112320108
PMCID: PMC3174582

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

Mapping the receptor site for alpha-scorpion toxins on a Na+ channel voltage sensor.PMID 21876146Read ↗

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

Mapping the interaction surface of scorpion β-toxins with an insect sodium channel.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 ↗

Evolutionary diversification of Mesobuthus α-scorpion toxins affecting sodium channels.Semantic proximity Read ↗

Elucidation of the molecular basis of selective recognition uncovers the interaction site for the core domain of scorpion alpha-toxins on sodium channels.Semantic proximity Read ↗

Mammalian skeletal muscle voltage-gated sodium channels are affected by scorpion depressant "insect-selective" toxins when preconditioned.Semantic proximity Read ↗

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

Beta-scorpion toxin effects suggest electrostatic interactions in domain II of voltage-dependent sodium channels.Semantic proximity Read ↗

Comparative study of the gating motif and C-type inactivation in prokaryotic voltage-gated sodium channels.Semantic proximity Read ↗

Tracking a complete voltage-sensor cycle with metal-ion bridges.Semantic proximity Read ↗

Docking of mu-conotoxin GIIIA in the sodium channel outer vestibule.Semantic proximity Read ↗

Nonsensing residues in S3-S4 linker's C terminus affect the voltage sensor set point in K+ channels.Semantic proximity Read ↗

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