Local constraints in either the GluN1 or GluN2 subunit equally impair NMDA receptor pore opening

@inproceedings{Talukder2011LocalCI,
  title={Local constraints in either the GluN1 or GluN2 subunit equally impair NMDA receptor pore opening},
  author={Iehab Talukder and Lonnie P Wollmuth},
  booktitle={The Journal of general physiology},
  year={2011}
}
The defining functional feature of N-methyl-d-aspartate (NMDA) receptors is activation gating, the energetic coupling of ligand binding into opening of the associated ion channel pore. NMDA receptors are obligate heterotetramers typically composed of glycine-binding GluN1 and glutamate-binding GluN2 subunits that gate in a concerted fashion, requiring all four ligands to bind for subsequent opening of the channel pore. In an individual subunit, the extracellular ligand-binding domain, composed… CONTINUE READING