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The Ν-methyl-d-aspartate (NMDA) receptor channel is an obligatory heterotetramer formed by two GluN1 and two GluN2 subunits. However, the differential contribution of the two different subunits to channel operation is not clear. We found that the apparent affinity of glycine to GluN1 (K gly ∼ 0.6 μM) is much higher than NMDA or glutamate to GluN2 (K NMDA ∼(More)
NMDA receptor channels are characterized by high Ca(2+) permeability. It remains unclear whether extracellular Ca(2+) could directly modulate channel gating and control Ca(2+) influxes. We demonstrate a pore-blocking site external to the activation gate for extracellular Ca(2+) and Cd(2+), which has the same charge and radius as Ca(2+) but is impermeable to(More)
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