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Rational Understanding of Nicotinic Receptors Drug Binding

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Abstract:

The atomic determination of the acetylcholine binding protein (AChBP), a molluscan cholinergic protein, homologous to the amino-terminal extracellular domain of nicotinic receptors (nAChRs), offers opportunities for the modeling of the acetylcholine binding site and its ligands. Recently, we constructed three-dimensional models of the Nterminal part of nAChR and docked in the putative ligand-binding pocket, different agonists (acetylcholine, nicotine and epibatidine) and antagonist (snake α-bungarotoxin). These hypothetical docking models offer a structural basis for rational design of drugs differentially binding to resting and active (or desensitized) conformations of the receptor site. These models thus pave the way to investigate, at the molecular level, the exciting challenge of the fast ion channel gating mechanisms by nicotinic agonists.

Keywords: allosteric transitions; drug design; nicotinic acetylcholine receptor; structure activity relationship

Document Type: Review Article

DOI: http://dx.doi.org/10.2174/1568026043451177

Affiliations: Institut Pasteur, URA 2182 CNRS “Recepteurs et Cognition”, Department of Biotechnologie, 25 rue du Dr. Roux, 75724 Paris Cedex 15, France.

Publication date: February 1, 2004

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