Energetic and structural interactions between delta-dendrotoxin and a voltage-gated potassium channel.

doi:10.1006/jmbi.2000.3522

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

Back to search

Article

Energetic and structural interactions between delta-dendrotoxin and a voltage-gated potassium channel.

Journal of molecular biology - 10 Mar 2000

Imredy J P, MacKinnon R

Abstract excerpt

Dendrotoxin proteins isolated from Mamba snake venom block potassium channels with a high degree of specificity and selectivity. Using site-directed mutagenesis we have identified residues that constitute the functional interaction surfaces of delta-dendrotoxin and its voltage-gated potassium channel receptor. delta-Dendrotoxin uses a triangular patch formed by seven side-chains (Lys3, Tyr4, Lys6, Leu7, Pro8,...

Topics

Amino Acid Sequence
Amino Acid Substitution
Animals
Binding Sites
Drosophila Proteins
Drosophila melanogaster
Elapid Venoms
Electrophysiology
Genetic Variation
Ion Channel Gating
Models, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Mutagenesis, Site-Directed

Oocytes

Potassium Channel Blockers

Potassium Channels

Protein Binding

Protein Conformation

Source

Open in PubMed

Identifiers

PMID: 10698633
DOI: 10.1006/jmbi.2000.3522

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Energetic and structural interactions between delta-dendrotoxin and a voltage-gated potassium channel.PMID 10698633Read ↗

The alpha-dendrotoxin footprint on a mammalian potassium channel.Semantic proximity Read ↗

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

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

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

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

Computational simulations of interactions of scorpion toxins with the voltage-gated potassium ion channel.Semantic proximity Read ↗

Discovery and characterisation of a novel toxin from Dendroaspis angusticeps, named Tx7335, that activates the potassium channel KcsA.Semantic proximity Read ↗

Modeling P-loops domain of sodium channel: homology with potassium channels and interaction with ligands.Semantic proximity Read ↗

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

Agitoxin footprinting the shaker potassium channel pore.Semantic proximity Read ↗

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

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