Allosteric interaction between the amino terminal domain and the ligand binding domain of NR2A

@article{Zheng2001AllostericIB,
  title={Allosteric interaction between the amino terminal domain and the ligand binding domain of NR2A},
  author={Fang Zheng and Kevin Erreger and C.-M. Low and Tue G Banke and Cheolju Lee and P Jeffrey Conn and Stephen F Traynelis},
  journal={Nature Neuroscience},
  year={2001},
  volume={4},
  pages={894-901}
}
Fast desensitization is an important regulatory mechanism of neuronal NMDA receptor function. Only recombinant NMDA receptors composed of NR1/NR2A exhibit a fast component of desensitization similar to neuronal NMDA receptors. Here we report that the fast desensitization of NR1/NR2A receptors is caused by ambient zinc, and that a positive allosteric interaction occurs between the extracellular zinc-binding site located in the amino terminal domain and the glutamate-binding domain of NR2A. The… CONTINUE READING

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