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

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.

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アイテムのパーマリンク: https://hdl.handle.net/21.11116/0000-0006-C5D4-C 版のパーマリンク: https://hdl.handle.net/21.11116/0000-000B-A9CA-3
資料種別: 学術論文

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 作成者:
Kudryashev, Misha1, 2, 著者                 
Castaño-Díez, Daniel1, 3, 著者
Deluz, Cédric4, 著者
Hassaine, Gherici4, 著者
Grasso, Luigino4, 著者
Graf-Meyer, Alexandra1, 著者
Vogel, Horst4, 著者
Stahlberg, Henning1, 著者
所属:
1Center for Cellular Imaging and NanoAnalytics (C-CINA), Biozentrum, University of Basel, Basel, Switzerland, ou_persistent22              
2Focal Area Infection Biology, Biozentrum, University of Basel, 4056 Basel, Switzerland, ou_persistent22              
3Scientific Computing Unit, Max Planck Institute for Brain Research, 60438 Frankfurt am Main, Germany, ou_persistent22              
4Ecole Polytechnique Fédérale de Lausanne (EPFL), Institute of Chemical Sciences and Engineering (ISIC), 1015 Lausanne, Switzerland, ou_persistent22              

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 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.

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言語: eng - English
 日付: 2015-10-052015-07-282015-11-082015-12-242016-01-05
 出版の状態: 出版
 ページ: 6
 出版情報: -
 目次: -
 査読: 査読あり
 識別子(DOI, ISBNなど): DOI: 10.1016/j.str.2015.11.004
 学位: -

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出版物 1

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出版物名: Structure
  その他 : Structure
種別: 学術雑誌
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出版社, 出版地: London : Cell Press
ページ: - 巻号: 24 (1) 通巻号: - 開始・終了ページ: 165 - 170 識別子(ISBN, ISSN, DOIなど): ISSN: 0969-2126
CoNE: https://pure.mpg.de/cone/journals/resource/954927002244_1