6BE1

Cryo-EM structure of serotonin receptor

6BE1 の概要

• エントリーDOI: 10.2210/pdb6be1/pdb
• EMDBエントリー: 7088
• 分子名称: 5-hydroxytryptamine receptor 3A, beta-D-mannopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (11 entities in total)
• 機能のキーワード: ion channel, membrane protein
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 274179.97

構造登録者

Basak, S.,Chakrapani, S. (登録日: 2017-10-24, 公開日: 2018-02-07, 最終更新日: 2024-10-23)

主引用文献

Basak, S.,Gicheru, Y.,Samanta, A.,Molugu, S.K.,Huang, W.,Fuente, M.,Hughes, T.,Taylor, D.J.,Nieman, M.T.,Moiseenkova-Bell, V.,Chakrapani, S.
Cryo-EM structure of 5-HT
Nat Commun, 9:514-514, 2018

PubMed Abstract: Serotonin receptors (5-HTR) directly regulate gut movement, and drugs that inhibit 5-HTR function are used to control emetic reflexes associated with gastrointestinal pathologies and cancer therapies. The 5-HTR function involves a finely tuned orchestration of three domain movements that include the ligand-binding domain, the pore domain, and the intracellular domain. Here, we present the structure from the full-length 5-HTR channel in the apo-state determined by single-particle cryo-electron microscopy at a nominal resolution of 4.3 Å. In this conformation, the ligand-binding domain adopts a conformation reminiscent of the unliganded state with the pore domain captured in a closed conformation. In comparison to the 5-HTR crystal structure, the full-length channel in the apo-conformation adopts a more expanded conformation of all the three domains with a characteristic twist that is implicated in gating.

PubMed: 29410406
DOI: 10.1038/s41467-018-02997-4

実験手法

ELECTRON MICROSCOPY (4.31 Å)