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Atomic insights into the physiological and functional diversity of NMDA receptors
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DOI：10.1016/j.tins.2026.05.004.png)
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Abstract
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Molecular insights into the atomic structures, subunit arrangements, and gating mechanisms of native NMDA receptors and AMPA receptors reveal the structural basis for their distinct biophysical and physiological properties during excitatory synaptic transmission. The distinct NMDA receptor subunit composition across various brain regions and neuron types provides clues into the diverse in vivo functions of native NMDA receptors. The intrinsic structural conformation, di- and tri-heteromeric assembly, and symmetric/asymmetric architectural transitions of NMDA receptor subtypes collectively determine their subtype-specific gating, biophysical profiles, and selective allosteric regulation. Variations in the binding pocket, affinity, and kinetics of NMDA receptor-targeting therapeutic drugs are key determinants of their distinct clinical efficacy and psychotomimetic side-effect profiles.
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