Ligand-specific deactivation time course of GluN1/GluN2D NMDA receptors

Katie M. Vance, Noriko Simorowski, Stephen F. Traynelis and Hiro Furukawa ()
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Katie M. Vance: Emory University School of Medicine, Rollins Research Center
Noriko Simorowski: Cold Spring Harbor Laboratory, Keck Structural Biology Laboratory
Stephen F. Traynelis: Emory University School of Medicine, Rollins Research Center
Hiro Furukawa: Cold Spring Harbor Laboratory, Keck Structural Biology Laboratory

Nature Communications, 2011, vol. 2, issue 1, 1-11

Abstract: Abstract N-methyl-D-aspartate (NMDA) receptors belong to the family of ionotropic glutamate receptors that mediate a majority of excitatory synaptic transmission. One unique property of GluN1/GluN2D NMDA receptors is an unusually prolonged deactivation time course following the removal of L-glutamate. Here we show, using x-ray crystallography and electrophysiology, that the deactivation time course of GluN1/GluN2D receptors is influenced by the conformational variability of the ligand-binding domain (LBD) as well as the structure of the activating ligand. L-glutamate and L-CCG-IV induce significantly slower deactivation time courses compared with other agonists. Crystal structures of the isolated GluN2D LBD in complex with various ligands reveal that the binding of L-glutamate induces a unique conformation at the backside of the ligand-binding site in proximity to the region at which the transmembrane domain would be located in the intact receptors. These data suggest that the activity of the GluN1/GluN2D NMDA receptor is controlled distinctively by the endogenous neurotransmitter L-glutamate.

Date: 2011
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DOI: 10.1038/ncomms1295

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