Abstract
Structures of pentameric ligand-gated channels (pLGIC) have now reached atomic resolution, with some members of the family also captured in multiple functional states. However, it is widely known that pLGIC gating is extensively modulated by membrane lipids. Using prokaryotic pLGIC homologues and chimeric channels, we probe the allosteric mechanism underlying these effects. Here we show by a combination of EPR spectroscopy, X-ray crystallography, and electrophysiology how lipids modulate function by altering the dynamics of transmembrane helices at the membrane-lipid interface.
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