5CFB

Crystal Structure of Human Glycine Receptor alpha-3 Bound to Strychnine

5CFB の概要

• エントリーDOI: 10.2210/pdb5cfb/pdb
• 分子名称: Glycine receptor subunit alpha-3,Glycine receptor subunit alpha-3, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, STRYCHNINE, ... (4 entities in total)
• 機能のキーワード: ligand-gated ion channel, neurotransmitter receptor, membrane protein, cys-loop receptor, transport protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 212471.50

構造登録者

Shaffer, P.L.,Huang, X.,Chen, H. (登録日: 2015-07-08, 公開日: 2015-09-30, 最終更新日: 2024-11-06)

主引用文献

Huang, X.,Chen, H.,Michelsen, K.,Schneider, S.,Shaffer, P.L.
Crystal structure of human glycine receptor-alpha 3 bound to antagonist strychnine.
Nature, 526:277-280, 2015

PubMed Abstract: Neurotransmitter-gated ion channels of the Cys-loop receptor family are essential mediators of fast neurotransmission throughout the nervous system and are implicated in many neurological disorders. Available X-ray structures of prokaryotic and eukaryotic Cys-loop receptors provide tremendous insights into the binding of agonists, the subsequent opening of the ion channel, and the mechanism of channel activation. Yet the mechanism of inactivation by antagonists remains unknown. Here we present a 3.0 Å X-ray structure of the human glycine receptor-α3 homopentamer in complex with a high affinity, high-specificity antagonist, strychnine. Our structure allows us to explore in detail the molecular recognition of antagonists. Comparisons with previous structures reveal a mechanism for antagonist-induced inactivation of Cys-loop receptors, involving an expansion of the orthosteric binding site in the extracellular domain that is coupled to closure of the ion pore in the transmembrane domain.

PubMed: 26416729
DOI: 10.1038/nature14972

実験手法

X-RAY DIFFRACTION (3.04 Å)