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JM Labriola, A Pandhare, M Jansen, MP Blanton, PJ Corringer and JE Baenziger
Abstract
Although the activity of the nicotinic acetylcholine receptor (nAChR) is exquisitely sensitive to its membrane environment, the underlying mechanisms remain poorly defined. The homologous prokaryotic pentameric ligand gated ion channel, GLIC, represents an excellent model for probing the molecular basis of nAChR sensitivity due to its high structural homology, ease of expression, and amenability to crystallographic analysis. We show here that membrane-reconstituted GLIC exhibits structural and biophysical properties similar to those of membrane-reconstituted nAChR, although GLIC is substantially more thermally stable. GLIC, however, does not possess the same exquisite lipid sensitivity. In particular, GLIC does not exhibit the same propensity to adopt an uncoupled conformation where agonist binding is uncoupled from channel gating. Structural comparisons provide insight into the chemical features that may predispose the nAChR to the formation of an uncoupled state.
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Concepts
Myasthenia gravis, Receptor, Ion channels, Muscarinic acetylcholine receptor, Acetylcholine receptor, Acetylcholine, Nicotinic acetylcholine receptor, Ligand-gated ion channel
MeSH headings
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