Cryo-EM structure of 5-HT3A receptor in its resting conformation

Serotonin receptor (5-HT3AR), a pentameric ligand-gated ion channel, regulates numerous gastrointestinal functions. Here the authors provide a cryo-electron microscopic structure from the full-length 5-HT3AR in the apo-state which corresponds to a resting conformation of the channel.

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Autores principales:	Sandip Basak, Yvonne Gicheru, Amrita Samanta, Sudheer Kumar Molugu, Wei Huang, Maria la de Fuente, Taylor Hughes, Derek J. Taylor, Marvin T. Nieman, Vera Moiseenkova-Bell, Sudha Chakrapani
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/1bb90dff34df4dafbd0d19b7edd091cb
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spelling	oai:doaj.org-article:1bb90dff34df4dafbd0d19b7edd091cb2021-12-02T16:49:23ZCryo-EM structure of 5-HT3A receptor in its resting conformation10.1038/s41467-018-02997-42041-1723https://doaj.org/article/1bb90dff34df4dafbd0d19b7edd091cb2018-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-02997-4https://doaj.org/toc/2041-1723Serotonin receptor (5-HT3AR), a pentameric ligand-gated ion channel, regulates numerous gastrointestinal functions. Here the authors provide a cryo-electron microscopic structure from the full-length 5-HT3AR in the apo-state which corresponds to a resting conformation of the channel.Sandip BasakYvonne GicheruAmrita SamantaSudheer Kumar MoluguWei HuangMaria la de FuenteTaylor HughesDerek J. TaylorMarvin T. NiemanVera Moiseenkova-BellSudha ChakrapaniNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Sandip Basak Yvonne Gicheru Amrita Samanta Sudheer Kumar Molugu Wei Huang Maria la de Fuente Taylor Hughes Derek J. Taylor Marvin T. Nieman Vera Moiseenkova-Bell Sudha Chakrapani Cryo-EM structure of 5-HT3A receptor in its resting conformation
description	Serotonin receptor (5-HT3AR), a pentameric ligand-gated ion channel, regulates numerous gastrointestinal functions. Here the authors provide a cryo-electron microscopic structure from the full-length 5-HT3AR in the apo-state which corresponds to a resting conformation of the channel.
format	article
author	Sandip Basak Yvonne Gicheru Amrita Samanta Sudheer Kumar Molugu Wei Huang Maria la de Fuente Taylor Hughes Derek J. Taylor Marvin T. Nieman Vera Moiseenkova-Bell Sudha Chakrapani
author_facet	Sandip Basak Yvonne Gicheru Amrita Samanta Sudheer Kumar Molugu Wei Huang Maria la de Fuente Taylor Hughes Derek J. Taylor Marvin T. Nieman Vera Moiseenkova-Bell Sudha Chakrapani
author_sort	Sandip Basak
title	Cryo-EM structure of 5-HT3A receptor in its resting conformation
title_short	Cryo-EM structure of 5-HT3A receptor in its resting conformation
title_full	Cryo-EM structure of 5-HT3A receptor in its resting conformation
title_fullStr	Cryo-EM structure of 5-HT3A receptor in its resting conformation
title_full_unstemmed	Cryo-EM structure of 5-HT3A receptor in its resting conformation
title_sort	cryo-em structure of 5-ht3a receptor in its resting conformation
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/1bb90dff34df4dafbd0d19b7edd091cb
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Cryo-EM structure of 5-HT3A receptor in its resting conformation

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