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Author Notes:

Correspondence to Stephen F. Traynelis: strayne@emory.edu

All authors wrote the manuscript.

Lesley C. Anson served as editor.

S.F. Traynelis is a consultant for Janssen Pharmaceuticals, Inc., the principal investigator on a research grant awarded to Emory University from Janssen Pharmaceuticals, a member of the Scientific Advisory Board for Sage Therapeutics, and co-founder of NeurOp, Inc.

K.B. Hansen is the principal investigator on a research grant awarded to University of Montana from Janssen Pharmaceuticals.

The other authors declare no competing financial interests.

Subjects:

Research Funding:

This work was supported by grants from National Institutes of Health to S.F. Traynelis (NS036654 and NS065371), K.B. Hansen (GM103546 and NS097536), and L.P. Wollmuth (NS088479).

Keywords:

  • Science & Technology
  • Life Sciences & Biomedicine
  • Physiology
  • D-ASPARTATE RECEPTORS
  • LIGAND-BINDING DOMAIN
  • CALCIUM-DEPENDENT INACTIVATION
  • AMINO-TERMINAL DOMAIN
  • AFFINITY ZINC INHIBITION
  • CEREBELLAR MOSSY FIBER
  • PARTIAL AGONIST ACTION
  • OUTSIDE-OUT PATCHES
  • PROTEIN-KINASE-A
  • GLUTAMATE-RECEPTOR

Structure, function, and allosteric modulation of NMDA receptors

Tools:

Journal Title:

Journal of General Physiology

Volume:

Volume 150, Number 8

Publisher:

, Pages 1081-1105

Type of Work:

Article | Final Publisher PDF

Abstract:

NMDA-type glutamate receptors are ligand-gated ion channels that mediate a Ca2+-permeable component of excitatory neurotransmission in the central nervous system (CNS). They are expressed throughout the CNS and play key physiological roles in synaptic function, such as synaptic plasticity, learning, and memory. NMDA receptors are also implicated in the pathophysiology of several CNS disorders and more recently have been identified as a locus for disease-associated genomic variation. NMDA receptors exist as a diverse array of subtypes formed by variation in assembly of seven subunits (GluN1, GluN2A-D, and GluN3A-B) into tetrameric receptor complexes. These NMDA receptor subtypes show unique structural features that account for their distinct functional and pharmacological properties allowing precise tuning of their physiological roles. Here, we review the relationship between NMDA receptor structure and function with an emphasis on emerging atomic resolution structures, which begin to explain unique features of this receptor.

Copyright information:

© 2018 Hansen et al.

This is an Open Access work distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International License (http://creativecommons.org/licenses/by-nc-sa/4.0/).

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