Title : Conformational rearrangement of the NMDA receptor amino-terminal domain during activation and allosteric modulation.

Pub. Date : 2021 May 11

PMID : 33976221






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Receptor activation involves glycine- and glutamate-stabilized closure of the GluN1 and GluN2 subunit ligand binding domains that is allosterically regulated by the amino-terminal domain (ATD). Glycine glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens
2 Glycine binding to GluN1 has no detectable effect, but unlocks the receptor for activation so that glycine and glutamate together drive an altered activation trajectory that is consistent with ATD dimer separation and rotation. Glycine glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens
3 Glycine binding to GluN1 has no detectable effect, but unlocks the receptor for activation so that glycine and glutamate together drive an altered activation trajectory that is consistent with ATD dimer separation and rotation. Glycine glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens