Title : Heteromerization of ligand binding domains of N-methyl-D-aspartate receptor requires both coagonists, L-glutamate and glycine.

Pub. Date : 2015 Jan 27

PMID : 25544544






3 Functional Relationships(s)
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1 We show herein that the ligand binding domains (LBD) of the GluN1 and GluN2A subunits of the NMDAR heterodimerize only when both coagonists, Glu and Gly/d-Ser, bind to their respective sites on GluN2 and GluN1. Glycine glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens
2 We show herein that the ligand binding domains (LBD) of the GluN1 and GluN2A subunits of the NMDAR heterodimerize only when both coagonists, Glu and Gly/d-Ser, bind to their respective sites on GluN2 and GluN1. Glycine glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens
3 Also, in a heteromer formed by the LBDs, GluN2A is more sensitized to bind Glu, while the affinity of Gly for GluN1 remains unchanged. Glycine glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens