B. Bettler, G.L. Collingridge, R. Dingledine, S.F.Heinemann, M. Hollmann, J. Lerma, D. Lodge, M. Mayer, M. Mishina, C. Mulle, S. Nakanishi, R. Olsen, S. Peineau, J.A. Peters, P. Seeburg, M. Spedding, and J.C. Watkins (2023).
Ionotropic glutamate receptors in GtoPdb v.2023.1.
UPHAR/BPS Guide to Pharmacology 2023(1).
doi: 10.2218/gtopdb/F75/2023.1
The ionotropic glutamate receptors comprise members of the NMDA (N-methyl-D-aspartate), AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazoleproprionic acid) and kainate receptor classes, named originally according to their preferred, synthetic, agonist. Receptor heterogeneity within each class arises from the homo-oligomeric, or hetero-oligomeric, assembly of distinct subunits into cation-selective tetramers. Each subunit of the tetrameric complex comprises an extracellular amino terminal domain (ATD), an extracellular ligand binding domain (LBD), 3 TM domains (M1, M3 and M4), a channel lining re-entrant 'p-loop' (M2) located between M1 and M3 and an intracellular carboxy- terminal domain (CTD). The X-ray structure of a homomeric ionotropic glutamate receptor (GluA2- see below) has recently been solved at 3.6 Â resolution and although providing the most complete structural information current available may not representative of the subunit arrangement of, for example, the heteromeric NMDA receptors. It is beyond the scope of this supplement to discuss the pharmacology of individual ionotropic glutamate receptor isoforms in detail; such information can be gleaned from. Agents that discriminate between subunit isoforms are, where appropriate, noted in the tables and additional compounds that distinguish between receptor isoforms are indicated in the text below.