[HTML][HTML] Conformational analysis of NMDA receptor GluN1, GluN2, and GluN3 ligand-binding domains reveals subtype-specific characteristics
The NMDA receptor family of glutamate receptor ion channels is formed by obligate
heteromeric assemblies of GluN1, GluN2, and GluN3 subunits. GluN1 and GluN3 bind
glycine, whereas GluN2 binds glutamate. Crystal structures of the GluN1 and GluN3A ligand-
binding domains (LBDs) in their apo states unexpectedly reveal open-and closed-cleft
conformations, respectively, with water molecules filling the binding pockets. Computed
conformational free energy landscapes for GluN1, GluN2A, and GluN3A LBDs reveal that …
heteromeric assemblies of GluN1, GluN2, and GluN3 subunits. GluN1 and GluN3 bind
glycine, whereas GluN2 binds glutamate. Crystal structures of the GluN1 and GluN3A ligand-
binding domains (LBDs) in their apo states unexpectedly reveal open-and closed-cleft
conformations, respectively, with water molecules filling the binding pockets. Computed
conformational free energy landscapes for GluN1, GluN2A, and GluN3A LBDs reveal that …
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