Structural basis of subtype-selective competitive antagonism for GluN2C/2D-containing NMDA receptors

Selectively inhibiting N-Methyl-D-aspartate receptors (NMDARs) containing the GluN2C/2D subunits has been challenging. Here, using electrophysiology and X-ray crystallography, authors show that compounds UBP791 and UBP1700 show over 40- and 50-fold selectivity for GluN2C/2D compared to GluN2A.

Bibliographic Details
Main Authors: Jue Xiang Wang, Mark W. Irvine, Erica S. Burnell, Kiran Sapkota, Robert J. Thatcher, Minjun Li, Noriko Simorowski, Arturas Volianskis, Graham L. Collingridge, Daniel T. Monaghan, David E. Jane, Hiro Furukawa
Format: Article
Language:English
Published: Nature Publishing Group 2020-01-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-020-14321-0
Description
Summary:Selectively inhibiting N-Methyl-D-aspartate receptors (NMDARs) containing the GluN2C/2D subunits has been challenging. Here, using electrophysiology and X-ray crystallography, authors show that compounds UBP791 and UBP1700 show over 40- and 50-fold selectivity for GluN2C/2D compared to GluN2A.
ISSN:2041-1723