2BJ0

Crystal Structure of AChBP from Bulinus truncatus revals the conserved structural scaffold and sites of variation in nicotinic acetylcholine receptors

2BJ0 の概要

• エントリーDOI: 10.2210/pdb2bj0/pdb
• 分子名称: ACETYLCHOLINE-BINDING PROTEIN, 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID (3 entities in total)
• 機能のキーワード: glycoprotein, glycprotein, igg fold, immunoglobulin domain, pentamer
• 由来する生物種: BULINUS TRUNCATUS
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 115429.73

構造登録者

Celie, P.H.N.,Klaassen, R.V.,Van Rossum-Fikkert, S.E.,Van Elk, R.,Van Nierop, P.,Smit, A.B.,Sixma, T.K. (登録日: 2005-01-27, 公開日: 2005-05-24, 最終更新日: 2024-10-23)

主引用文献

Celie, P.H.N.,Klaassen, R.V.,Van Rossum-Fikkert, S.E.,Van Elk, R.,Van Nierop, P.,Smit, A.B.,Sixma, T.K.
Crystal Structure of Acetylcholine-Binding Protein from Bulinus Truncatus Reveals the Conserved Structural Scaffold and Sites of Variation in Nicotinic Acetylcholine Receptors.
J.Biol.Chem., 280:26457-, 2005

PubMed Abstract: 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.

PubMed: 15899893
DOI: 10.1074/JBC.M414476200

実験手法

X-RAY DIFFRACTION (2 Å)