2bj0: Difference between revisions

The crystal structure of acetylcholine-binding protein (AChBP) from the, mollusk Lymnaea stagnalis is the established model for the ligand binding, domains of the ligand-gated ion channel family, which includes nicotinic, acetylcholine, 5-hydroxytryptamine (5-HT3), gamma-aminobutyric acid, (GABA), types A and C, and glycine receptors. 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 amino acid changes in the binding site contribute to a 5-10-fold, difference in affinity for nicotinic ligands. Comparison of these, structures will be valuable for improving structure-function studies of, ligand-gated ion channel receptors, including signal transduction, homology modeling, and drug design.

2BJ0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bulinus_truncatus Bulinus truncatus] with CXS as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BJ0 OCA].  

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