A conserved glycine harboring disease-associated mutations permits NMDA receptor slow deactivation and high Ca2+ permeability

Little is known about the impact of de novo and inherited missense mutations in the NMDA receptor M4 transmembrane helices. In this study, the authors use functional and computational approaches to demonstrate how mutations to conserved glycine sites within this region cause structural rearrangement...

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Autores principales:	Johansen B. Amin, Xiaoling Leng, Aaron Gochman, Huan-Xiang Zhou, Lonnie P. Wollmuth
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/9165b88c892d4963b2756c84424dfbcc
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spelling	oai:doaj.org-article:9165b88c892d4963b2756c84424dfbcc2021-12-02T15:34:17ZA conserved glycine harboring disease-associated mutations permits NMDA receptor slow deactivation and high Ca2+ permeability10.1038/s41467-018-06145-w2041-1723https://doaj.org/article/9165b88c892d4963b2756c84424dfbcc2018-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-06145-whttps://doaj.org/toc/2041-1723Little is known about the impact of de novo and inherited missense mutations in the NMDA receptor M4 transmembrane helices. In this study, the authors use functional and computational approaches to demonstrate how mutations to conserved glycine sites within this region cause structural rearrangement, altered receptor deactivation and calcium permeability.Johansen B. AminXiaoling LengAaron GochmanHuan-Xiang ZhouLonnie P. WollmuthNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Johansen B. Amin Xiaoling Leng Aaron Gochman Huan-Xiang Zhou Lonnie P. Wollmuth A conserved glycine harboring disease-associated mutations permits NMDA receptor slow deactivation and high Ca2+ permeability
description	Little is known about the impact of de novo and inherited missense mutations in the NMDA receptor M4 transmembrane helices. In this study, the authors use functional and computational approaches to demonstrate how mutations to conserved glycine sites within this region cause structural rearrangement, altered receptor deactivation and calcium permeability.
format	article
author	Johansen B. Amin Xiaoling Leng Aaron Gochman Huan-Xiang Zhou Lonnie P. Wollmuth
author_facet	Johansen B. Amin Xiaoling Leng Aaron Gochman Huan-Xiang Zhou Lonnie P. Wollmuth
author_sort	Johansen B. Amin
title	A conserved glycine harboring disease-associated mutations permits NMDA receptor slow deactivation and high Ca2+ permeability
title_short	A conserved glycine harboring disease-associated mutations permits NMDA receptor slow deactivation and high Ca2+ permeability
title_full	A conserved glycine harboring disease-associated mutations permits NMDA receptor slow deactivation and high Ca2+ permeability
title_fullStr	A conserved glycine harboring disease-associated mutations permits NMDA receptor slow deactivation and high Ca2+ permeability
title_full_unstemmed	A conserved glycine harboring disease-associated mutations permits NMDA receptor slow deactivation and high Ca2+ permeability
title_sort	conserved glycine harboring disease-associated mutations permits nmda receptor slow deactivation and high ca2+ permeability
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/9165b88c892d4963b2756c84424dfbcc
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A conserved glycine harboring disease-associated mutations permits NMDA receptor slow deactivation and high Ca2+ permeability

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