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

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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Bibliographic Details
Main Authors: Johansen B. Amin, Xiaoling Leng, Aaron Gochman, Huan-Xiang Zhou, Lonnie P. Wollmuth
Format: Article
Language:English
Published: Nature Publishing Group 2018-09-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-018-06145-w
Description
Summary: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.
ISSN:2041-1723

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