Related ArticlesNMR structures of the transmembrane domains of the ?4?2 nAChR.
Biochim Biophys Acta. 2012 May;1818(5):1261-8
Authors: Bondarenko V, Mowrey D, Tillman T, Cui T, Liu LT, Xu Y, Tang P
Abstract
The ?4?2 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 ?4?2 and other neuronal nAChRs is presently limited. In this study, we determined structures of the transmembrane (TM) domains of the ?4 and ?2 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 ?4 and ?2 interacted with each other and spontaneously formed pentameric assemblies in the LDAO micelles. The Na(+) flux assay revealed that ?4?2 formed Na(+) permeable channels in lipid vesicles. Efflux of Na(+) through the ?4?2 channels reduced intra-vesicle Sodium Green™ fluorescence in a time-dependent manner that was not observed in vesicles without incorporating ?4?2. The study provides structural insight into the TM domains of the ?4?2 nAChR. It offers a valuable structural framework for rationalizing extensive biochemical data collected previously on the ?4?2 nAChR and for designing new therapeutic modulators.
[NMR paper] First Solution Structures of Seven-Transmembrane Helical Proteins
From Mendeley Biomolecular NMR group:
First Solution Structures of Seven-Transmembrane Helical Proteins
Angewandte Chemie International Edition (2011). Pages: n/a-n/a. Oliver Zerbe et al.
Published using Mendeley: Academic software for researchers
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Unravelling the Conformational Plasticity of the Extracellular Domain of a Prokaryotic nAChR Homologue in Solution by NMR
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http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi201223u/aop/images/medium/bi-2011-01223u_0002.gif
Biochemistry
DOI: 10.1021/bi201223u
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Bacterial expression, purification, and model membrane reconstitution of the transmembrane and cytoplasmic domains of the human APP binding protein LR11/SorLA for NMR studies.
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NMR structures of the transmembrane domains of the ?4?2 nAChR.
Linear Mode
