Molecular mechanism of setron-mediated inhibition of full-length 5-HT3A receptor

Serotonin receptors (5-HT3R) belong to the pentameric ligand-gated ion channel superfamily and mediate excitatory postsynaptic signaling. Here the authors present the high-resolution cryo-EM structure of 5-HT3AR bound with the competitive antagonist granisetron and further validate the granisetron-b...

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Autores principales:	Sandip Basak, Yvonne Gicheru, Abhijeet Kapoor, Megan L. Mayer, Marta Filizola, Sudha Chakrapani
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/b766ed4a222d442488eb15a659c8ec8c
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spelling	oai:doaj.org-article:b766ed4a222d442488eb15a659c8ec8c2021-12-02T16:58:04ZMolecular mechanism of setron-mediated inhibition of full-length 5-HT3A receptor10.1038/s41467-019-11142-82041-1723https://doaj.org/article/b766ed4a222d442488eb15a659c8ec8c2019-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-11142-8https://doaj.org/toc/2041-1723Serotonin receptors (5-HT3R) belong to the pentameric ligand-gated ion channel superfamily and mediate excitatory postsynaptic signaling. Here the authors present the high-resolution cryo-EM structure of 5-HT3AR bound with the competitive antagonist granisetron and further validate the granisetron-binding mode with electrophysiology measurements and MD simulations.Sandip BasakYvonne GicheruAbhijeet KapoorMegan L. MayerMarta FilizolaSudha ChakrapaniNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-11 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Sandip Basak Yvonne Gicheru Abhijeet Kapoor Megan L. Mayer Marta Filizola Sudha Chakrapani Molecular mechanism of setron-mediated inhibition of full-length 5-HT3A receptor
description	Serotonin receptors (5-HT3R) belong to the pentameric ligand-gated ion channel superfamily and mediate excitatory postsynaptic signaling. Here the authors present the high-resolution cryo-EM structure of 5-HT3AR bound with the competitive antagonist granisetron and further validate the granisetron-binding mode with electrophysiology measurements and MD simulations.
format	article
author	Sandip Basak Yvonne Gicheru Abhijeet Kapoor Megan L. Mayer Marta Filizola Sudha Chakrapani
author_facet	Sandip Basak Yvonne Gicheru Abhijeet Kapoor Megan L. Mayer Marta Filizola Sudha Chakrapani
author_sort	Sandip Basak
title	Molecular mechanism of setron-mediated inhibition of full-length 5-HT3A receptor
title_short	Molecular mechanism of setron-mediated inhibition of full-length 5-HT3A receptor
title_full	Molecular mechanism of setron-mediated inhibition of full-length 5-HT3A receptor
title_fullStr	Molecular mechanism of setron-mediated inhibition of full-length 5-HT3A receptor
title_full_unstemmed	Molecular mechanism of setron-mediated inhibition of full-length 5-HT3A receptor
title_sort	molecular mechanism of setron-mediated inhibition of full-length 5-ht3a receptor
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/b766ed4a222d442488eb15a659c8ec8c
work_keys_str_mv	AT sandipbasak molecularmechanismofsetronmediatedinhibitionoffulllength5ht3areceptor AT yvonnegicheru molecularmechanismofsetronmediatedinhibitionoffulllength5ht3areceptor AT abhijeetkapoor molecularmechanismofsetronmediatedinhibitionoffulllength5ht3areceptor AT meganlmayer molecularmechanismofsetronmediatedinhibitionoffulllength5ht3areceptor AT martafilizola molecularmechanismofsetronmediatedinhibitionoffulllength5ht3areceptor AT sudhachakrapani molecularmechanismofsetronmediatedinhibitionoffulllength5ht3areceptor
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Molecular mechanism of setron-mediated inhibition of full-length 5-HT3A receptor

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