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Crystal Structure of Acetylcholine-binding Protein from Bulinus truncatus Reveals the Conserved Structural Scaffold and Sites of

By Variation Nicotinic and Acetylcholine Receptors


The crystal structure of acetylcholine-binding protein (AChBP) from the mollusk Lymnaea stagnalis is the es-tablished model for the ligand binding domains of the ligand-gated ion channel family, which includes nico-tinic acetylcholine, 5-hydroxytryptamine (5-HT3), -ami-nobutyric acid (GABA), types A and C, and glycine re-ceptors. Here we present the crystal structure of a remote homolog, AChBP from Bulinus truncatus, which reveals both the conserved structural scaffold and the sites of variation in this receptor family. These include rigid body movements of loops that are close to the transmembrane interface in the receptors and changes in the intermonomer contacts, which alter the pentamer stability drastically. Structural, pharmacological and mutational analysis of both AChBPs shows how 3 amin

Year: 2005
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