The Structure of the Mouse Serotonin 5-HT3 Receptor in Lipid Vesicles

Kudryashev, Misha; Castaño-Díez, Daniel; Deluz, Cédric; Hassaine, Gherici; Grasso, Luigino; Graf-Meyer, Alexandra; Vogel, Horst; Stahlberg, Henning

doi:10.1016/j.str.2015.11.004

アイテム詳細

登録内容を編集ファイル形式で保存

一時保存へ追加

タグ情報を表示リリース履歴を表示詳細要約

公開

学術論文

The Structure of the Mouse Serotonin 5-HT3 Receptor in Lipid Vesicles

MPS-Authors

There are no MPG-Authors in the publication available

External Resource

There are no locators available

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

フルテキスト (公開)

公開されているフルテキストはありません

付随資料 (公開)

There is no public supplementary material available

引用

Kudryashev, M., Castaño-Díez, D., Deluz, C., Hassaine, G., Grasso, L., Graf-Meyer, A., Vogel, H., & Stahlberg, H. (2016). The Structure of the Mouse Serotonin 5-HT3 Receptor in Lipid Vesicles. Structure, 24(1), 165-170. doi:10.1016/j.str.2015.11.004.

引用: https://hdl.handle.net/21.11116/0000-0006-C5D4-C

要旨

The function of membrane proteins is best understood if their structure in the lipid membrane is known. Here, we determined the structure of the mouse serotonin 5-HT₃ receptor inserted in lipid bilayers to a resolution of 12 Å without stabilizing antibodies by cryo electron tomography and subtomogram averaging. The reconstruction reveals protein secondary structure elements in the transmembrane region, the extracellular pore, and the transmembrane channel pathway, showing an overall similarity to the available X-ray model of the truncated 5-HT₃ receptor determined in the presence of a stabilizing nanobody. Structural analysis of the 5-HT₃ receptor embedded in a lipid bilayer allowed the position of the membrane to be determined. Interactions between the densely packed receptors in lipids were visualized, revealing that the interactions were maintained by the short horizontal helices. In combination with methodological improvements, our approach enables the structural analysis of membrane proteins in response to voltage and ligand gating.