2bj0

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{{STRUCTURE_2bj0| PDB=2bj0 | SCENE= }}
{{STRUCTURE_2bj0| PDB=2bj0 | SCENE= }}
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'''CRYSTAL STRUCTURE OF ACHBP FROM BULINUS TRUNCATUS REVALS THE CONSERVED STRUCTURAL SCAFFOLD AND SITES OF VARIATION IN NICOTINIC ACETYLCHOLINE RECEPTORS'''
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===CRYSTAL STRUCTURE OF ACHBP FROM BULINUS TRUNCATUS REVALS THE CONSERVED STRUCTURAL SCAFFOLD AND SITES OF VARIATION IN NICOTINIC ACETYLCHOLINE RECEPTORS===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_15899893}}
==About this Structure==
==About this Structure==
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[[Category: Pentamer]]
[[Category: Pentamer]]
[[Category: Signal]]
[[Category: Signal]]
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Revision as of 20:45, 27 July 2008

Image:2bj0.png

Template:STRUCTURE 2bj0

CRYSTAL STRUCTURE OF ACHBP FROM BULINUS TRUNCATUS REVALS THE CONSERVED STRUCTURAL SCAFFOLD AND SITES OF VARIATION IN NICOTINIC ACETYLCHOLINE RECEPTORS

Template:ABSTRACT PUBMED 15899893

About this Structure

2BJ0 is a Single protein structure of sequence from Bulinus truncatus. Full crystallographic information is available from OCA.

Reference

Crystal structure of acetylcholine-binding protein from Bulinus truncatus reveals the conserved structural scaffold and sites of variation in nicotinic acetylcholine receptors., Celie PH, Klaassen RV, van Rossum-Fikkert SE, van Elk R, van Nierop P, Smit AB, Sixma TK, J Biol Chem. 2005 Jul 15;280(28):26457-66. Epub 2005 May 16. PMID:15899893

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