Ionotropic glutamate receptor

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Lig_chan
TCDB
1.A.10
OPM superfamily8
OPM protein3kg2
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Ionotropic glutamate receptors (iGluRs) are

NMDA receptors and delta receptors (see below).[2]

AMPA receptors are the main charge carriers during basal transmission, permitting influx of

ions and therefore only permit ion flux following prior depolarisation. This enables them to act as coincidence detectors for synaptic plasticity. Calcium influx through NMDA receptors leads to persistent modifications in the strength of synaptic transmission.[3][4]

iGluRs are tetramers (they are formed of four subunits). All subunits have a shared architecture with four domain layers: two extracellular clamshell domains called the N-terminal domain (NTD) and ligand-binding domain (LBD; which binds glutamate), the transmembrane domain (TMD) that forms the ion channel, and an intracellular C-terminal domain (CTD).[5]

Human proteins/genes encoding iGluR subunits

AMPA receptors: GluA1/GRIA1; GluA2/GRIA2; GluA3/GRIA3; GluA4/GRIA4;

delta receptors: GluD1/GRID1; GluD2/GRID2;

kainate receptors: GluK1/GRIK1; GluK2/GRIK2; GluK3/GRIK3; GluK4/GRIK4; GluK5/GRIK5;

NMDA receptors: GluN1/GRIN1; GluN2A/GRIN2A; GluN2B/GRIN2B; GluN2C/GRIN2C; GluN2D/GRIN2D; GluN3A/GRIN3A; GluN3B/GRIN3B;

References