4D01

Crystal Structure of the Extracellular Domain of the Human Alpha9 Nicotinic Acetylcholine Receptor

4D01 の概要

• エントリーDOI: 10.2210/pdb4d01/pdb
• 関連するPDBエントリー: 4UXU 4UY2
• 分子名称: NEURONAL ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA-9, 2-acetamido-2-deoxy-beta-D-glucopyranose, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: signaling protein, ligand binding domain, cys-loop receptor
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25997.72

構造登録者

Giastas, P.,Zouridakis, M.,Zarkadas, E.,Tzartos, S.J. (登録日: 2014-04-23, 公開日: 2014-10-01, 最終更新日: 2024-10-09)

主引用文献

Zouridakis, M.,Giastas, P.,Zarkadas, E.,Chroni-Tzartou, D.,Bregestovski, P.,Tzartos, S.J.
Crystal Structures of Free and Antagonist-Bound States of Human Alpha9 Nicotinic Receptor Extracellular Domain
Nat.Struct.Mol.Biol., 21:976-, 2014

PubMed Abstract: We determined the X-ray crystal structures of the extracellular domain (ECD) of the monomeric state of human neuronal α9 nicotinic acetylcholine receptor (nAChR) and of its complexes with the antagonists methyllycaconitine and α-bungarotoxin at resolutions of 1.8 Å, 1.7 Å and 2.7 Å, respectively. The structure of the monomeric α9 ECD superimposed well with the structures of homologous proteins in pentameric assemblies, denoting native folding, despite the absence of a complementary subunit and transmembrane domain. The interaction motifs of both antagonists were similar to those in the complexes with homologous pentameric proteins, thus highlighting the major contribution of the principal side of α9 ECD to their binding. The structures revealed a functionally important β7-β10 strand interaction in α9-containing nAChRs, involving their unique Thr147, a hydration pocket similar to that of mouse α1 ECD and a membrane-facing network coordinated by the invariant Arg210.

PubMed: 25282151
DOI: 10.1038/NSMB.2900

実験手法

X-RAY DIFFRACTION (1.795 Å)