Title : Modulation of glycine potency in rat recombinant NMDA receptors containing chimeric NR2A/2D subunits expressed in Xenopus laevis oocytes.

Pub. Date : 2008 Jan 1

PMID : 17962328






3 Functional Relationships(s)
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Protein Name
Organism
1 Heteromeric NMDARs are composed of coagonist glycine-binding NR1 subunits and glutamate-binding NR2 subunits. Glycine glutamate ionotropic receptor NMDA type subunit 1 L homeolog Xenopus laevis
2 This heterogeneity is specified by the particular NR2 subunit within the NMDAR complex since the glycine-binding NR1 subunit is common to all NMDARs investigated. Glycine glutamate ionotropic receptor NMDA type subunit 1 L homeolog Xenopus laevis
3 We conclude that the variation in glycine potency is caused by interactions between the NR1 and NR2 ligand-binding domains that occur following agonist binding and which may be involved in the initial conformation changes that determine channel gating. Glycine glutamate ionotropic receptor NMDA type subunit 1 L homeolog Xenopus laevis