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

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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Bibliographic Details
Main Authors: Vojtech Vyklicky, Cherise Stanley, Chris Habrian, Ehud Y. Isacoff
Format: Article
Language:English
Published: Nature Portfolio 2021-05-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-021-23024-z

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