Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 433, Issue 17, Pages -Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2021.167128
Keywords
Structure; Gating; GLIC; Nicotinic acetylcholine receptor; Glycine receptor
Categories
Funding
- Knut and Alice Wallenberg Foundation
- Swedish Research Council
- Swedish e-Science Research Centre
- Molecular Biophysics Stockholm research environment
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The superfamily of pentameric ligand-gated ion channels plays crucial roles in electrochemical signal transduction across evolution, with increasing structural studies focusing on three model subfamilies. Common themes include gating mechanisms and diversity beyond the protein level.
The superfamily of pentameric ligand-gated ion channels (pLGICs) comprises key players in electrochemical signal transduction across evolution, including historic model systems for receptor allostery and targets for drug development. Accordingly, structural studies of these channels have steadily increased, and now approach 250 depositions in the protein data bank. This review contextualizes currently available structures in the pLGIC family, focusing on morphology, ligand binding, and gating in three model subfamilies: the prokaryotic channel GLIC, the cation-selective nicotinic acetylcholine receptor, and the anion-selective glycine receptor. Common themes include the challenging process of capturing and annotating channels in distinct functional states; partially conserved gating mechanisms, including remodeling at the extracellular/transmembrane-domain interface; and diversity beyond the protein level, arising from post-translational modifications, ligands, lipids, and signaling partners. Interpreting pLGIC structures can be compared to describing an elephant in the dark, relying on touch alone to comprehend the many parts of a monumental beast: each structure represents a snapshot in time under specific experimental conditions, which must be integrated with further structure, function, and simulations data to build a comprehensive model, and understand how one channel may fundamentally differ from another. (C) 2021 The Author(s). Published by Elsevier Ltd.
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