An NMDA receptor gating mechanism developed from MD simulations reveals molecular details underlying subunit-specific contributions.

@article{Dai2013AnNR,
  title={An NMDA receptor gating mechanism developed from MD simulations reveals molecular details underlying subunit-specific contributions.},
  author={Jian Cheng Dai and Huan-Xiang Zhou},
  journal={Biophysical journal},
  year={2013},
  volume={104 10},
  pages={
          2170-81
        }
}
N-methyl-D-aspartate (NMDA) receptors are obligate heterotetrameric ligand-gated ion channels that play critical roles in learning and memory. Here, using targeted molecular dynamics simulations, we developed an atomistic model for the gating of the GluN1/GluN2A NMDA receptor. Upon agonist binding, lobe closure of the ligand-binding domain produced outward pulling of the M3-D2 linkers, leading to outward movements of the C-termini of the pore-lining M3 helices and opening of the channel. The… CONTINUE READING

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