Skip to Main content Skip to Navigation
Journal articles

Structural Sensitivity of a Prokaryotic Pentameric Ligand-gated Ion Channel to Its Membrane Environment

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, Gloebacter ligand-gated ion channel (GLIC), represents an excellent model for probing the molecular basis of nAChR sensitivity because of its high structural homology, relative ease of expression, and amenability to crystallographic analysis. We show here that membrane-reconstituted GLIC exhibits structural and biophysical properties similar to those of the 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.
Document type :
Journal articles
Complete list of metadatas

https://hal-pasteur.archives-ouvertes.fr/pasteur-01721776
Contributor : Ana Cova Rodrigues <>
Submitted on : Friday, March 2, 2018 - 3:25:22 PM
Last modification on : Monday, January 13, 2020 - 5:08:10 PM

Links full text

Identifiers

Collections

Citation

Jonathan Labriola, Akash Pandhare, Michael Jansen, Michael Blanton, Pierre-Jean Corringer, et al.. Structural Sensitivity of a Prokaryotic Pentameric Ligand-gated Ion Channel to Its Membrane Environment. Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2013, 288 (16), pp.11294 - 11303. ⟨10.1074/jbc.M113.458133⟩. ⟨pasteur-01721776⟩

Share

Metrics

Record views

126