Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10767218 | Biochemical and Biophysical Research Communications | 2007 | 6 Pages |
Abstract
We investigate the interactions between the long chain α-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.
Keywords
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Biochemistry
Authors
Maria Konstantakaki, Jean-Pierre Changeux, Antoine Taly,