Mechanisms of activation and desensitization of full-length glycine receptor in lipid nanodiscs

Glycinergic synapses play a central role in motor control and pain processing in the central nervous system. Here, authors present cryo-EM structures of the full-length glycine receptors (GlyRs) reconstituted into lipid nanodiscs in the unliganded, glycine-bound and allosteric modulator-bound confor...

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Autores principales:	Arvind Kumar, Sandip Basak, Shanlin Rao, Yvonne Gicheru, Megan L. Mayer, Mark S. P. Sansom, Sudha Chakrapani
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/dcf52f74a2044b09b3777a173af38405
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spelling	oai:doaj.org-article:dcf52f74a2044b09b3777a173af384052021-12-02T18:46:58ZMechanisms of activation and desensitization of full-length glycine receptor in lipid nanodiscs10.1038/s41467-020-17364-52041-1723https://doaj.org/article/dcf52f74a2044b09b3777a173af384052020-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-17364-5https://doaj.org/toc/2041-1723Glycinergic synapses play a central role in motor control and pain processing in the central nervous system. Here, authors present cryo-EM structures of the full-length glycine receptors (GlyRs) reconstituted into lipid nanodiscs in the unliganded, glycine-bound and allosteric modulator-bound conformations and reveal global conformational changes underlying GlyR channel gating and modulation.Arvind KumarSandip BasakShanlin RaoYvonne GicheruMegan L. MayerMark S. P. SansomSudha ChakrapaniNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Arvind Kumar Sandip Basak Shanlin Rao Yvonne Gicheru Megan L. Mayer Mark S. P. Sansom Sudha Chakrapani Mechanisms of activation and desensitization of full-length glycine receptor in lipid nanodiscs
description	Glycinergic synapses play a central role in motor control and pain processing in the central nervous system. Here, authors present cryo-EM structures of the full-length glycine receptors (GlyRs) reconstituted into lipid nanodiscs in the unliganded, glycine-bound and allosteric modulator-bound conformations and reveal global conformational changes underlying GlyR channel gating and modulation.
format	article
author	Arvind Kumar Sandip Basak Shanlin Rao Yvonne Gicheru Megan L. Mayer Mark S. P. Sansom Sudha Chakrapani
author_facet	Arvind Kumar Sandip Basak Shanlin Rao Yvonne Gicheru Megan L. Mayer Mark S. P. Sansom Sudha Chakrapani
author_sort	Arvind Kumar
title	Mechanisms of activation and desensitization of full-length glycine receptor in lipid nanodiscs
title_short	Mechanisms of activation and desensitization of full-length glycine receptor in lipid nanodiscs
title_full	Mechanisms of activation and desensitization of full-length glycine receptor in lipid nanodiscs
title_fullStr	Mechanisms of activation and desensitization of full-length glycine receptor in lipid nanodiscs
title_full_unstemmed	Mechanisms of activation and desensitization of full-length glycine receptor in lipid nanodiscs
title_sort	mechanisms of activation and desensitization of full-length glycine receptor in lipid nanodiscs
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/dcf52f74a2044b09b3777a173af38405
work_keys_str_mv	AT arvindkumar mechanismsofactivationanddesensitizationoffulllengthglycinereceptorinlipidnanodiscs AT sandipbasak mechanismsofactivationanddesensitizationoffulllengthglycinereceptorinlipidnanodiscs AT shanlinrao mechanismsofactivationanddesensitizationoffulllengthglycinereceptorinlipidnanodiscs AT yvonnegicheru mechanismsofactivationanddesensitizationoffulllengthglycinereceptorinlipidnanodiscs AT meganlmayer mechanismsofactivationanddesensitizationoffulllengthglycinereceptorinlipidnanodiscs AT markspsansom mechanismsofactivationanddesensitizationoffulllengthglycinereceptorinlipidnanodiscs AT sudhachakrapani mechanismsofactivationanddesensitizationoffulllengthglycinereceptorinlipidnanodiscs
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Mechanisms of activation and desensitization of full-length glycine receptor in lipid nanodiscs

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