ArticleBiochimica et biophysica acta2012
NMR structures of the transmembrane domains of the α4β2 nAChR.
Article in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 39 citations in OpenAlex.
- Mechanism of NACHO-mediated assembly of pentameric ligand-gated ion channels.bioRxiv : the preprint server for biology · 2024Article
- A release of local subunit conformational heterogeneity underlies gating in a muscle nicotinic acetylcholine receptor.Nature communications · 2024Article
- Triple arginines as molecular determinants for pentameric assembly of the intracellular domain of 5-HTThe Journal of general physiology · 2019Article
- Structural basis of neurosteroid anesthetic action on GABANature communications · 2018Article
- Solution NMR Studies of Anesthetic Interactions with Ion Channels.Methods in enzymology · 2018Article
- Pentameric quaternary structure of the intracellular domain of serotonin type 3A receptors.Scientific reports · 2016Article
- Conformational Changes Underlying Desensitization of the Pentameric Ligand-Gated Ion Channel ELIC.Structure (London, England : 1993) · 2015Article
- Functional Chimeras of GLIC Obtained by Adding the Intracellular Domain of Anion- and Cation-Conducting Cys-Loop Receptors.Biochemistry · 2015Article
- Atomistic insights into human Cys-loop receptors by solution NMR.Biochimica et biophysica acta · 2015Article
- Side-chain conformation at the selectivity filter shapes the permeation free-energy landscape of an ion channel.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- NMR structures of membrane proteins in phospholipid bilayers.Quarterly reviews of biophysics · 2014Review
- NMR structures of the human α7 nAChR transmembrane domain and associated anesthetic binding sites.Biochimica et biophysica acta · 2014Article
- Identifying barbiturate binding sites in a nicotinic acetylcholine receptor with [3H]allyl m-trifluoromethyldiazirine mephobarbital, a photoreactive barbiturate.Molecular pharmacology · 2014Article
- Molecular interactions between mecamylamine enantiomers and the transmembrane domain of the human α4β2 nicotinic receptor.Biochemistry · 2014Article
- Photoaffinity labeling the propofol binding site in GLIC.Biochemistry · 2014Article
- Seeking structural specificity: direct modulation of pentameric ligand-gated ion channels by alcohols and general anesthetics.Pharmacological reviews · 2014Review
- Insights into distinct modulation of α7 and α7β2 nicotinic acetylcholine receptors by the volatile anesthetic isoflurane.The Journal of biological chemistry · 2013Article
- Assessment of homology templates and an anesthetic binding site within the γ-aminobutyric acid receptor.Anesthesiology · 2013Article
- Open-channel structures of the human glycine receptor α1 full-length transmembrane domain.Structure (London, England : 1993) · 2013Article
- NMR resolved multiple anesthetic binding sites in the TM domains of the α4β2 nAChR.Biochimica et biophysica acta · 2013Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
The α4β2 nicotinic acetylcholine receptor (nAChR) is the predominant heteromeric subtype of nAChRs in the brain, which has been implicated in numerous neurological conditions. The structural information specifically for the α4β2 and other neuronal nAChRs is presently limited. In this study, we determined structures of the transmembrane (TM) domains of the α4 and β2 subunits in lauryldimethylamine-oxide (LDAO) micelles using solution NMR spectroscopy. NMR experiments and size exclusion chromatography-multi-angle light scattering (SEC-MALS) analysis demonstrated that the TM domains of α4 and β2 interacted with each other and spontaneously formed pentameric assemblies in the LDAO micelles. The Na(+) flux assay revealed that α4β2 formed Na(+) permeable channels in lipid vesicles. Efflux of Na(+) through the α4β2 channels reduced intra-vesicle Sodium Green™ fluorescence in a time-dependent manner that was not observed in vesicles without incorporating α4β2. The study provides structural insight into the TM domains of the α4β2 nAChR. It offers a valuable structural framework for rationalizing extensive biochemical data collected previously on the α4β2 nAChR and for designing new therapeutic modulators.
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