Conformational rearrangement of the NMDA receptor amino-terminal domain during activation and allosteric modulation

N-Methyl-D-aspartate receptors (NMDARs) activation involves closure of the GluN1 and GluN2 subunit ligand binding domains, which is regulated allosterically by the amino-terminal domain (ATD). Here, smFRET, used to monitor conformational rearrangements of the NMDAR ATD, reveals that glutamate bindin...

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Autores principales:	Vojtech Vyklicky, Cherise Stanley, Chris Habrian, Ehud Y. Isacoff
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/8e4c29ebad794dcf8259b791a65adee9
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spelling	oai:doaj.org-article:8e4c29ebad794dcf8259b791a65adee92021-12-02T16:57:57ZConformational rearrangement of the NMDA receptor amino-terminal domain during activation and allosteric modulation10.1038/s41467-021-23024-z2041-1723https://doaj.org/article/8e4c29ebad794dcf8259b791a65adee92021-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-23024-zhttps://doaj.org/toc/2041-1723N-Methyl-D-aspartate receptors (NMDARs) activation involves closure of the GluN1 and GluN2 subunit ligand binding domains, which is regulated allosterically by the amino-terminal domain (ATD). Here, smFRET, used to monitor conformational rearrangements of the NMDAR ATD, reveals that glutamate binding to GluN2 subunits elicits two identical, sequential steps of ATD dimer separation that are regulated by protons.Vojtech VyklickyCherise StanleyChris HabrianEhud Y. IsacoffNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Vojtech Vyklicky Cherise Stanley Chris Habrian Ehud Y. Isacoff Conformational rearrangement of the NMDA receptor amino-terminal domain during activation and allosteric modulation
description	N-Methyl-D-aspartate receptors (NMDARs) activation involves closure of the GluN1 and GluN2 subunit ligand binding domains, which is regulated allosterically by the amino-terminal domain (ATD). Here, smFRET, used to monitor conformational rearrangements of the NMDAR ATD, reveals that glutamate binding to GluN2 subunits elicits two identical, sequential steps of ATD dimer separation that are regulated by protons.
format	article
author	Vojtech Vyklicky Cherise Stanley Chris Habrian Ehud Y. Isacoff
author_facet	Vojtech Vyklicky Cherise Stanley Chris Habrian Ehud Y. Isacoff
author_sort	Vojtech Vyklicky
title	Conformational rearrangement of the NMDA receptor amino-terminal domain during activation and allosteric modulation
title_short	Conformational rearrangement of the NMDA receptor amino-terminal domain during activation and allosteric modulation
title_full	Conformational rearrangement of the NMDA receptor amino-terminal domain during activation and allosteric modulation
title_fullStr	Conformational rearrangement of the NMDA receptor amino-terminal domain during activation and allosteric modulation
title_full_unstemmed	Conformational rearrangement of the NMDA receptor amino-terminal domain during activation and allosteric modulation
title_sort	conformational rearrangement of the nmda receptor amino-terminal domain during activation and allosteric modulation
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/8e4c29ebad794dcf8259b791a65adee9
work_keys_str_mv	AT vojtechvyklicky conformationalrearrangementofthenmdareceptoraminoterminaldomainduringactivationandallostericmodulation AT cherisestanley conformationalrearrangementofthenmdareceptoraminoterminaldomainduringactivationandallostericmodulation AT chrishabrian conformationalrearrangementofthenmdareceptoraminoterminaldomainduringactivationandallostericmodulation AT ehudyisacoff conformationalrearrangementofthenmdareceptoraminoterminaldomainduringactivationandallostericmodulation
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Conformational rearrangement of the NMDA receptor amino-terminal domain during activation and allosteric modulation

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