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Updated: Jul 14, 2026

Localization of Plasma Membrane and Intracellular Neuronal Nicotinic Acetylcholine Receptors Using Quantitative Imaging in Mammalian Cells
Published on: December 19, 2025
Docking of alpha-cobratoxin suggests a basal conformation of the nicotinic receptor
Maria Konstantakaki1, Jean-Pierre Changeux, Antoine Taly
1Recepteurs et Cognition, Unité de Recherche Associée, Centre National de la Recherche Scientifique 2182, Institut Pasteur, Paris, France.
Abstract:
We investigate the interactions between the long chain alpha-cobratoxin (Cbtx) and the nicotinic acetylcholine receptor using a rigid body docking procedure. The method, (i) reproduces the binding of Cbtx to Lymnea acetylcholine-binding protein (AChBP); (ii) shows that most of the structures of AChBP obtained in the presence of antagonists are compatible with Cbtx binding; and (iii) reveals a complex between Cbtx and muscle nAChR that corresponds to the basal "resting" state conformation. The structures are made available for further understanding of the allosteric transitions of the nAChR as well as for drug design.
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