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This Article Full Text Full Text (PDF) All Versions of this Article: 584/3/727    most recent jphysiol.2007.142554v1 Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Gay, E. A. Articles by Yakel, J. L. Search for Related Content PubMed PubMed Citation Articles by Gay, E. A. Articles by Yakel, J. L. Related Collections Review articles

¹ Laboratory of Neurobiology, National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human Services, PO Box 12233, Research Triangle Park, NC 27709, USA

Nicotinic acetylcholine receptors (nAChRs) are in the superfamily of Cys-loop ligand-gated ion channels, and are pentameric assemblies of five subunits, with each subunit arranged around the central ion-conducting pore. The binding of ACh to the extracellular interface between two subunits induces channel opening. With the recent 4 Å resolution of the Torpedo nAChR, and the crystal structure of the related molluscan ACh binding protein, much has been learned about the structure of the ligand binding domain and the channel pore, as well as major structural rearrangements that may confer channel opening. For example, the putative pathway coupling agonist binding to channel gating may include a major rearrangement of the C-loop within the ligand binding pocket, and the disruption of a salt bridge between an arginine residue at the end of the β10 strand and a glutamate residue in the β1–β2 linker. Here we will review and discuss the latest structural findings aiming to further refine the transduction pathway linking binding to gating for the nAChR channels, and discuss similarities and differences among the different members of this Cys-loop superfamily of receptors.

(Received 6 August 2007; accepted after revision 3 September 2007; first published online 6 September 2007)
Corresponding author J. L. Yakel: NIEHS, F2-08, PO Box 12233, 111 T.W. Alexander Drive, Research Triangle Park, N.C. 27709, USA. Email: yakel{at}niehs.nih.gov

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