Skip to Main content Skip to Navigation
Journal articles

Pore conformations and gating mechanism of a Cys-loop receptor.

Abstract : Neurons regulate the propagation of chemoelectric signals throughout the nervous system by opening and closing ion channels, a process known as gating. Here, histidine-based metal-binding sites were engineered along the intrinsic pore of a chimeric Cys-loop receptor to probe state-dependent Zn(2+)-channel interactions. Patterns of Zn(2+) ion binding within the pore reveal that, in the closed state, the five pore-lining segments adopt an oblique orientation relative to the axis of ion conduction and constrict into a physical gate at their intracellular end. The interactions of Zn(2+) with the open state indicate that the five pore-lining segments should rigidly tilt to enable the movement of their intracellular ends away from the axis of ion conduction, so as to open the constriction (i.e., the gate). Alignment of the functional results with the 3D structure of an acetylcholine receptor allowed us to generate structural models accounting for the closed and open pore conformations and for a gating mechanism of a Cys-loop receptor.
Document type :
Journal articles
Complete list of metadatas

https://hal-pasteur.archives-ouvertes.fr/pasteur-00162520
Contributor : Yolande Meunier <>
Submitted on : Friday, July 13, 2007 - 4:06:46 PM
Last modification on : Wednesday, September 23, 2020 - 10:44:03 AM

Links full text

Identifiers

Collections

Citation

Yoav Paas, Gilad Gibor, Regis Grailhe, Nathalie Savatier-Duclert, Virginie Dufresne, et al.. Pore conformations and gating mechanism of a Cys-loop receptor.. Proceedings of the National Academy of Sciences of the United States of America , National Academy of Sciences, 2005, 102 (44), pp.15877-82. ⟨10.1073/pnas.0507599102⟩. ⟨pasteur-00162520⟩

Share

Metrics

Record views

370