Extended Data Fig. 2: Structural analysis of agonist-bound GluN1a-2B NMDARs.
From: Structural insights into binding of therapeutic channel blockers in NMDA receptors
a, Overall cryo-EM density of the agonist-bound rat GluN1a-2B NMDAR (GluN1a and GluN2B in magenta and forest, respectively). b, EM density of the bound glycine (left) and glutamate (right) at LBD of GluN1a and GluN2B, respectively. c, Zoom-in view of the channel blocker binding cavity at the TMD where there is no density (left). The binding site has three layers, Thr ring (GluN1a-Thr648 GluN2B-Thr647) at the channel gate, the hydrophobic ring (GluN1a-Val644 and GluN1a-Ala645 and GluN2B-Leu643 and GluN2B-Ala644), and the Asn ring (GluN1a-Asn616 and GluN2B-Asn615). d, Domain organization and functional state. The agonist-bound GluN1a-2B NMDAR here has similarity to the non-active1 conformation of GluN1b-2B NMDAR (gray, PDBID: 6WHS) with the similar ATD and LBD orientations and extent of separation between the LBD-TMD linkers of GluN2B (spheres = GluN2B-Gln662).
