Introduction of GRIK3
Glutamate receptors are composed of Ionotropic glutamate receptors (iGluRs) and metabotropic glutamate receptors (mGluRs). GRIK3 is a subunit of iGluRs, belonging to the subfamily of kainate receptors. Kainate receptors are further classified into low-affinity receptor families (GRIK1-GRIK3) and high-affinity receptor families (GRIK4-GRIK5) based on their affinity for the neurotoxin kainic acid. GRIK3 can coassemble with either GRIK4 or GRIK5 to form heteromeric receptors and act as an excitatory neurotransmitter at many synapses in the central nervous system. GRIK3 has multiple isoforms derived from alternative splicing and RNA editing. Two splice variants of GRIK3 have been identified, GRIK3a and GRIK3b, in which almost the entire C-terminus of GRIK3a is replaced by an unrelated sequence of 55 amino acids.
|Basic Information of GRIK3|
|Protein Name||Glutamate receptor ionotropic, kainate 3|
|Organism||Homo sapiens (Human)|
Functions of GRIK3 Membrane Protein
The kainate receptors are the least studied subfamily of iGluRs. These receptors are thought to have a neuromodulatory role and have been associated with a variety of disorders in the central nervous system, such as epilepsy. This makes kainate receptors interesting potential drug targets. The kainite receptors have been identified to play multiple roles in neuronal plasticity, including both short- and long-term plasticity. Agonists, antagonists, and allosteric modulators have been developed targeting these kainite receptors. Some pyrrolilquinoxalinedione derivatives have been found to behave as potent anticonvulsants in the kindling model, such as the LU97175, which displays an extremely high selectivity for GRIK1 and GRIK2 and, especially, for GRIK3. Still, much of the function and molecular mechanisms of GRIK3 remain to be elucidated in the future.
Fig.1 Scheme of kainite receptor subunits. (Pinheiro, 2006)
Application of GRIK3 Membrane Protein in Literature
This article reported structures of GluK3 ligand binding domain in complex with two 2,4-syn-functionalized (S)-glutamate analogues to investigate their structural potential as chemical scaffolds.
This study reported that zinc binding to GluK3 stabilized the GluK3 dimer interface, slowed desensitization, and potentiated currents, providing a mechanism for kainite receptor potentiation at glutamatergic synapses.
This article determined the high-resolution crystal structures of the GluK3 and GluK5 amino-terminal domains (ATDs). Moreover, this study also helped strengthen the structure and function of GluK4-GluK5, the least understood family of iGluRs.
This article investigated the X-ray structure of the ligand-binding domain of GluK3 in complex with glutamate for the first time.
This article investigated the effects of some of the GluK1 antagonists on currents mediated by recombinant homomeric GluK3 and heteromeric GluK2/3 receptors.
GRIK3 Preparation Options
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