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

Efficient binding of 4/7 α-conotoxins to nicotinic α4β2 receptors is prevented by Arg185 and Pro195 in the α4 subunit.

Molecular pharmacology - 1 Oct 2012

Beissner Mirko, Dutertre Sébastien, Schemm Rudolf, Danker Timm, Sporning Annett, Grubmüller Helmut, Nicke Annette

Abstract excerpt

α-Conotoxins are subtype-selective nicotinic acetylcholine receptor (nAChR) antagonists. Although potent α3β2 nAChR-selective α-conotoxins have been identified, currently characterized α-conotoxins show no or only weak affinity for α4β2 nAChRs, which are, besides α7 receptors, the most abundant nAChRs in the mammalian brain. To identify the determinants responsible for this difference, we substituted selected...

Read the complete abstract on PubMed

Topics

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

Share to Acetylcholine
Share to Molecular Docking Simulation

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

Share to Nicotinic Agonists

Share to Oocytes

Share to Patch-Clamp Techniques

Share to Protein Subunits

Share to Receptors, Nicotinic

Share to Xenopus laevis

Source

Identifiers

PMID: 22802270
DOI: 10.1124/mol.112.078683

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

Efficient binding of 4/7 α-conotoxins to nicotinic α4β2 receptors is prevented by Arg185 and Pro195 in the α4 subunit.PMID 22802270Read ↗

Basic Residues at Position 11 of α-Conotoxin LvIA Influence Subtype Selectivity between α3β2 and α3β4 Nicotinic Receptors via an Electrostatic Mechanism.Semantic proximity Read ↗

Beta2 subunit contribution to 4/7 alpha-conotoxin binding to the nicotinic acetylcholine receptor.Semantic proximity Read ↗

Key residues in the nicotinic acetylcholine receptor β2 subunit contribute to α-conotoxin LvIA binding.Semantic proximity Read ↗

αO-Conotoxin GeXIVA disulfide bond isomers exhibit differential sensitivity for various nicotinic acetylcholine receptors but retain potency and selectivity for the human α9α10 subtype.Semantic proximity Read ↗

Effect of Methionine Oxidation and Substitution of α-Conotoxin TxID on α3β4 Nicotinic Acetylcholine Receptor.Semantic proximity Read ↗

Synthetic α-conotoxin mutants as probes for studying nicotinic acetylcholine receptors and in the development of novel drug leads.Semantic proximity Read ↗

Erabutoxin mutants demonstrate interface selectivity at human fetal and adult muscle-type nicotinic acetylcholine receptors.Semantic proximity Read ↗

α-Conotoxin PeIA[S9H,V10A,E14N] potently and selectively blocks α6β2β3 versus α6β4 nicotinic acetylcholine receptors.Semantic proximity Read ↗

Single amino acid substitutions modulate the function of α9α10 nicotinic acetylcholine receptor.Semantic proximity Read ↗

Structural determinants for alpha-neurotoxin sensitivity in muscle nAChR and their implications for the gating mechanism.Semantic proximity Read ↗

The Allosteric Activation of α7 nAChR by α-Conotoxin MrIC Is Modified by Mutations at the Vestibular Site.Semantic proximity Read ↗

Specificity determinants of allosteric modulation in the neuronal nicotinic acetylcholine receptor: a fine line between inhibition and potentiation.Semantic proximity Read ↗

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