3SH1

Ac-AChBP ligand binding domain mutated to human alpha-7 nAChR

3SH1 の概要

• エントリーDOI: 10.2210/pdb3sh1/pdb
• 関連するPDBエントリー: 2BYR 3SIO 3T4M
• 分子名称: Soluble acetylcholine receptor, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (10 entities in total)
• 機能のキーワード: human nicotinic acetylcholine receptor binding protein, methyllycaconitine binding, glycosylation, receptor
• 由来する生物種: Aplysia californica (California sea hare)
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 276076.31

構造登録者

Nemecz, A.,Taylor, P.W. (登録日: 2011-06-15, 公開日: 2011-10-26, 最終更新日: 2024-10-30)

主引用文献

Nemecz, A.,Taylor, P.
Creating an alpha-7 nicotinic acetylcholine recognition domain from the acetylcholine binding protein: crystallographic and ligand selectivity analyses
J.Biol.Chem., 286:42555-42565, 2011

PubMed Abstract: Determining the structure of the ligand-binding domain of the nicotinic acetylcholine receptor (nAChR) has been a long standing goal in the design of selective drugs useful in implicated diseases for this prevalent receptor family. Acetylcholine-binding proteins have proven to be valuable surrogates with structural similarity and sequence identity to the extracellular domain of the nicotinic receptor, yet these soluble proteins have their unique features and do not serve as exact replicates of the nAChRs of interest. Here we systematically modify the sequence of these proteins toward the homomeric human α7 nAChR. These chimeric proteins exhibit a shift in affinities to reflect α7 binding characteristics yet maintain expression levels and stability conducive for crystallization. We also present a pentameric humanoid nAChR extracellular domain with the structural determination of the α7 nAChR glycosylation site.

PubMed: 22009746
DOI: 10.1074/jbc.M111.286583

実験手法

X-RAY DIFFRACTION (2.9 Å)