ArticleBiochemistry2006
Determinants of alpha-conotoxin BuIA selectivity on the nicotinic acetylcholine receptor beta subunit.
Article in Biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Analogs of α-conotoxin PnIC selectively inhibit α7β2- over α7-only subtype nicotinic acetylcholine receptors via a novel allosteric mechanism.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024Article
- Characterization of an α 4/7-Conotoxin LvIF fromMarine drugs · 2021Article
- Interactions of the α3β2 Nicotinic Acetylcholine Receptor Interfaces with α-Conotoxin LsIA and its Carboxylated C-terminus Analogue: Molecular Dynamics Simulations.Marine drugs · 2020Article
- α-Conotoxins active at α3-containing nicotinic acetylcholine receptors and their molecular determinants for selective inhibition.British journal of pharmacology · 2018Review
- Structural mechanisms for α-conotoxin activity at the human α3β4 nicotinic acetylcholine receptor.Scientific reports · 2017Article
- Key Structural Determinants in the Agonist Binding Loops of Human β2 and β4 Nicotinic Acetylcholine Receptor Subunits Contribute to α3β4 Subtype Selectivity of α-Conotoxins.The Journal of biological chemistry · 2016Article
- Structural and Functional Characterization of a Novel α-Conotoxin Mr1.7 from Conus marmoreus Targeting Neuronal nAChR α3β2, α9α10 and α6/α3β2β3 Subtypes.Marine drugs · 2015Article
- Molecular interaction of α-conotoxin RgIA with the rat α9α10 nicotinic acetylcholine receptor.Molecular pharmacology · 2015Article
- Key residues in the nicotinic acetylcholine receptor β2 subunit contribute to α-conotoxin LvIA binding.The Journal of biological chemistry · 2015Article
- Alanine scan of α-conotoxin RegIIA reveals a selective α3β4 nicotinic acetylcholine receptor antagonist.The Journal of biological chemistry · 2015Article
- Discovery of a potent and selective α3β4 nicotinic acetylcholine receptor antagonist from an α-conotoxin synthetic combinatorial library.Journal of medicinal chemistry · 2014Article
- Identifying key amino acid residues that affect α-conotoxin AuIB inhibition of α3β4 nicotinic acetylcholine receptors.The Journal of biological chemistry · 2013Article
- α6 nAChR subunit residues that confer α-conotoxin BuIA selectivity.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2012Article
- Molecular basis for the differential sensitivity of rat and human α9α10 nAChRs to α-conotoxin RgIA.Journal of neurochemistry · 2012Article
- α-Conotoxin BuIA[T5A;P6O]: a novel ligand that discriminates between α6ß4 and α6ß2 nicotinic acetylcholine receptors and blocks nicotine-stimulated norepinephrine release.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2010Article
- Atypical alpha-conotoxin LtIA from Conus litteratus targets a novel microsite of the alpha3beta2 nicotinic receptor.The Journal of biological chemistry · 2010Article
- Alpha-conotoxins as pharmacological probes of nicotinic acetylcholine receptors.Acta pharmacologica Sinica · 2009Review
- High throughput electrophysiology with Xenopus oocytes.Combinatorial chemistry & high throughput screening · 2009Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Neuronal nicotinic acetylcholine receptors (nAChRs) are pentamers composed of alpha and beta subunits. Different molecular compositions of these subunits constitute various receptor subtypes that are implicated in the pathophysiology and/or treatment of several disease states but are difficult to distinguish pharmacologically. Alpha-conotoxins are a group of small, structurally defined peptides that may be used to molecularly dissect the nAChR-binding site. Heteromeric nAChRs generally contain either a beta2 or beta4 subunit in addition to an alpha subunit at the ligand-binding interface. Alpha-conotoxin BuIA kinetically distinguishes between beta2- and beta4-containing nAChRs, with long off times for the latter. Mutational studies were used to assess the influence of residues that line the putative acetylcholine-binding pocket but differ between beta2 and beta4 subunits. Residues Thr/Lys59, Val/Ile111, and Phe/Gln119 of the respective beta2 and beta4 subunits are critical to off-rate differences. Among these residues, Thr59 of nAChR beta2 may interfere with effective access to the binding site, whereas Lys59 may facilitate this binding.
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