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© Marie Prévost, Institut Pasteur
Image of a portion of a Xenopus oocyte expressing a channel receptor.
Publication : The Journal of biological chemistry

Structural sensitivity of a prokaryotic pentameric ligand-gated ion channel to its membrane environment

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in The Journal of biological chemistry - 05 Mar 2013

Labriola JM, Pandhare A, Jansen M, Blanton MP, Corringer PJ, Baenziger JE

Link to Pubmed [PMID] – 23463505

J. Biol. Chem. 2013 Apr;288(16):11294-303

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.

http://www.ncbi.nlm.nih.gov/pubmed/23463505