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Structure, function, and allosteric modulation of NMDA receptors

Hansen, KB; Yi, F; Perszyk, RE; Furukawa, H; Wollmuth, LP; Gibb, AJ; Traynelis, SF; (2018) Structure, function, and allosteric modulation of NMDA receptors. The Journal of General Physiology , 150 (7) pp. 1081-1105. 10.1085/jgp.201812032. Green open access

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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.

Type: Article
Title: Structure, function, and allosteric modulation of NMDA receptors
Location: United States
Open access status: An open access version is available from UCL Discovery
DOI: 10.1085/jgp.201812032
Publisher version: http://jgp.rupress.org/content/150/8/1081/tab-arti...
Language: English
Additional information: © 2018 Hansen et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).
Keywords: Protein Structure and Dynamics, Molecular Physiology, Molecular Pharmacology
UCL classification: UCL
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Neuro, Physiology and Pharmacology
URI: https://discovery.ucl.ac.uk/id/eprint/10053787
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