6ove
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Crystal structure of GluN1/GluN2A NMDA receptor agonist binding domains with glycine and antagonist, 4-propylphenyl-ACEPC
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Structural highlights
FunctionNMDZ1_RAT NMDA receptor subtype of glutamate-gated ion channels possesses high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. Plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. It mediates neuronal functions in glutamate neurotransmission. Is involved in the cell surface targeting of NMDA receptors.[1] See AlsoReferences
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This page was last modified 07:17, 11 October 2023.