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6Y59

5-HT3A receptor in Salipro (apo, C5 symmetric)

6Y59 の概要
エントリーDOI10.2210/pdb6y59/pdb
関連するPDBエントリー6Y5A 6Y5B
EMDBエントリー10691 10692 10693
分子名称5-hydroxytryptamine receptor 3A (1 entity in total)
機能のキーワードpentameric ligand-gated ion channel, plgic, serotonin 5-ht3a receptor, 5-ht3ar, salipro, membrane protein
由来する生物種Mus musculus (House mouse)
タンパク質・核酸の鎖数5
化学式量合計303340.43
構造登録者
Zhang, Y.,Dijkman, P.M.,Zou, R.,Zandl-Lang, M.,Sanchez, R.M.,Eckhardt-Strelau, L.,Koefeler, H.,Vogel, H.,Yuan, S.,Kudryashev, M. (登録日: 2020-02-25, 公開日: 2020-12-23, 最終更新日: 2024-10-23)
主引用文献Zhang, Y.,Dijkman, P.M.,Zou, R.,Zandl-Lang, M.,Sanchez, R.M.,Eckhardt-Strelau, L.,Kofeler, H.,Vogel, H.,Yuan, S.,Kudryashev, M.
Asymmetric opening of the homopentameric 5-HT 3A serotonin receptor in lipid bilayers.
Nat Commun, 12:1074-1074, 2021
Cited by
PubMed Abstract: Pentameric ligand-gated ion channels (pLGICs) of the Cys-loop receptor family are key players in fast signal transduction throughout the nervous system. They have been shown to be modulated by the lipid environment, however the underlying mechanism is not well understood. We report three structures of the Cys-loop 5-HT serotonin receptor (5HTR) reconstituted into saposin-based lipid bilayer discs: a symmetric and an asymmetric apo state, and an asymmetric agonist-bound state. In comparison to previously published 5HTR conformations in detergent, the lipid bilayer stabilises the receptor in a more tightly packed, 'coupled' state, involving a cluster of highly conserved residues. In consequence, the agonist-bound receptor conformation adopts a wide-open pore capable of conducting sodium ions in unbiased molecular dynamics (MD) simulations. Taken together, we provide a structural basis for the modulation of 5HTR by the membrane environment, and a model for asymmetric activation of the receptor.
PubMed: 33594077
DOI: 10.1038/s41467-021-21016-7
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (3.2 Å)
構造検証レポート
Validation report summary of 6y59
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-07-30に公開中

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