We suggest that the higher efficacy of DCS at NR1/NR2C receptors involves structural rearrangements at the dimer interface and an effect on NR1/NR2C receptor pregating conformational changes..     ///    "To relate the structural rearrangements to receptor gating, we recorded single-channel currents from outside-out patches containing a single active NR1/NR2C receptor. "    ///    Structural determinants of D-cycloserine efficacy at the NR1/NR2C NMDA receptors..     ///    DCS increased the mean open time and open probability of NR1/NR2C receptors compared with glycine.     ///    The most pronounced differences were observed in the NR1/NR2C simulation between the orientation of helices F and G of the NR1 subunit.     ///    DCS shows partial agonism at NR1/NR2B but has higher relative efficacy than glycine at NR1/NR2C receptor.     ///    Molecular dynamics (MD) simulations of the NR1/NR2B and NR1/NR2C agonist binding domain dimer suggest only subtle differences in the interactions of DCS with NR1 binding site residues relative to glycine.     ///    Maximum likelihood fitting of a gating model for NR1/NR2C receptor activation to the single-channel data suggests that DCS specifically accelerates the rate constant governing a fast gating step and reduces the closing rate. 