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

Mutating a critical lysine in ShK toxin alters its binding configuration in the pore-vestibule region of the voltage-gated potassium channel, Kv1.3.

Biochemistry - 8 Oct 2002

Lanigan Mark D, Kalman Katalin, Lefievre Yann, Pennington Michael W, Chandy K George, Norton Raymond S

Abstract excerpt

The voltage-gated potassium channel in T lymphocytes, Kv1.3, an important target for immunosuppressants, is blocked by picomolar concentrations of the polypeptide ShK toxin and its analogue ShK-Dap22. ShK-Dap22 shows increased selectivity for Kv1.3, and our goal was to determine the molecular basis for this selectivity by probing the interactions of ShK and ShK-Dap22 with the pore and vestibule of Kv1.3. The free...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Ligands

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

Share to Lysine

Share to Potassium Channels

Share to Potassium Channels, Voltage-Gated

Share to Protein Conformation

Share to Protein Structure, Tertiary

Share to Thermodynamics

Source

Identifiers

PMID: 12356296
DOI: 10.1021/bi026400b

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

Mutating a critical lysine in ShK toxin alters its binding configuration in the pore-vestibule region of the voltage-gated potassium channel, Kv1.3.PMID 12356296Read ↗

Revealing the architecture of a K+ channel pore through mutant cycles with a peptide inhibitor.Semantic proximity Read ↗

Energetic and structural interactions between delta-dendrotoxin and a voltage-gated potassium channel.Semantic proximity Read ↗

The scorpion toxin BeKm-1 blocks hERG cardiac potassium channels using an indispensable arginine residue.Semantic proximity Read ↗

Why does the inner-helix mutation A413C double the stoichiometry of Kv1.3 channel block by emopamil but not by verapamil?Semantic proximity Read ↗

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

Molecular simulation of the interaction of kappa-conotoxin-PVIIA with the Shaker potassium channel pore.Semantic proximity Read ↗

Identification of a novel pharmacophore for peptide toxins interacting with K+ channels.Semantic proximity Read ↗

Modeling the structure of agitoxin in complex with the Shaker K+ channel: a computational approach based on experimental distance restraints extracted from thermodynamic mutant cycles.Semantic proximity Read ↗

A variable residue in the pore of Kv1 channels is critical for the high affinity of blockers from sea anemones and scorpions.Semantic proximity Read ↗

Chemical tuning reveals a cation-π gating bridge between the voltage-sensor and pore domains in the Kv7.1 potassium channel.Semantic proximity Read ↗

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

Coupling of S4 helix translocation and S6 gating analyzed by molecular-dynamics simulations of mutated Kv channels.Semantic proximity Read ↗

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