Figure 1.
Regulatory landscape of GluN1–GluN2 NMDA receptors. Canonical NMDARs assemble as heterotetrameric ion channels comprising two GluN1 (light pink) and two GluN2 (light teal) subunits, which bind glycine and glutamate, respectively. Representative PAMs/NAMs, along with open-channel blockers (shown as spheres or chemical structures), are positioned at their corresponding regulatory sites. Structural models for GluN1 and GluN2 were adapted from PDB ID 7SAA. Ifenprodil, PYD-106, DQP-997-74, and TCN-201 occupy distinct sites within the extracellular domain, while PS engages a juxtamembrane lipid-facing pocket. In contrast, classic open-channel blockers, such as phencyclidine (PCP), lodge within the transmembrane ion-conducting pathway. TMD, transmembrane domain.

Regulatory landscape of GluN1–GluN2 NMDA receptors. Canonical NMDARs assemble as heterotetrameric ion channels comprising two GluN1 (light pink) and two GluN2 (light teal) subunits, which bind glycine and glutamate, respectively. Representative PAMs/NAMs, along with open-channel blockers (shown as spheres or chemical structures), are positioned at their corresponding regulatory sites. Structural models for GluN1 and GluN2 were adapted from PDB ID 7SAA. Ifenprodil, PYD-106, DQP-997-74, and TCN-201 occupy distinct sites within the extracellular domain, while PS engages a juxtamembrane lipid-facing pocket. In contrast, classic open-channel blockers, such as phencyclidine (PCP), lodge within the transmembrane ion-conducting pathway. TMD, transmembrane domain.

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