Glutamate Receptor Related Drug Discovery Products
Membrane protein stable cell lines are widely used in many areas of biomedical research. Creative Biolabs can offer membrane protein stable cell lines to stablish in vitro models for High Throughput Screening.
Creative Biolabs offers high-quality, innovative tools to help research groups accelerate membrane protein drug discovery. They can be found by targets. If there is no product that meets your needs, please contact us.
The majority of excitatory synapses respond via the glutamate receptor ion channels (iGluRs), which are widely expressed in the brain and spinal cord. There are 18 genes that together make up the four main families of mammalian iGluRs: AMPA, kainate, NMDA, and delta receptors. In vivo, several different receptor subtypes are produced by the coassembly of iGluRs within families but not across them. One important element that has aided in the structural research of iGluRs is their distinctive design. The ligand-binding cores of iGluRs are separate domains, one of which is present in each subunit, in contrast to the cys-loop receptors, in which ligand-binding sites are created at the interface between subunits.
Fig.1. Domain structure in iGluRs. (Mayer, 2005)
Creative Biolabs is confident in providing the customers with the best glutamate receptor related tools while at the most competitive price:
Overview of Glutamate Receptor
The tetrameric complexes of subunits that make up glutamate receptors arise exclusively through the assembly of subunits belonging to the same functional receptor class. Based on pharmacology and structural homology, glutamate receptors are divided into four different classes: AMPA receptors (GluA1-GluA4), kainate receptors (GluK1-GluK5), NMDA receptors (GluN1, GluN2A-GluN2D, GluN3A, and GluN3B), and δ receptors (GluD1 and GluD2). The GluA1 to GluA4 AMPA receptor subunits can combine to create homo- and heteromers. The kainate receptor subunits GluK1 to GluK3 also form homo- and heteromers, whereas GluK4 and GluK5 only coexpress with GluK1 to GluK3 to create functional receptors. Both in native cells and in heterologous expression methods, the GluD1 and GluD2 receptors can assemble into homomeric receptors but do not appear to be able to combine with the AMPA, kainate, or NMDA receptor subunits to form heteromers. Additionally, it appears that neither GluD1 nor GluD2 can develop receptors that can be triggered by any known agoni.
Fig.2. Structure of the GluA2 AMPA receptor. (Traynelis, 2010)
Glutamate Receptor Drug Discovery
A whole new structural era has begun in the study of glutamate receptors. A prospective target for modifying neuronal and glial function for therapeutic benefit in an incredibly broad spectrum of neurological diseases is the gating machinery at all glutamate receptors. Further knowledge that contributes to clarifying the function of glutamate receptors in both healthy processes like learning and memory as well as in sickness includes how cells regulate synaptic glutamate receptor function and govern localization. The very real possibility of ground-breaking medications expanding therapy options for many patients coincides with this advancement.
References
- Mayer, M. L. Glutamate receptor ion channels. Current opinion in neurobiology. 2005, 15(3): 282-288.
- Traynelis, S.F.; et al. Glutamate receptor ion channels: structure, regulation, and function. Pharmacological reviews. 2010, 62(3): 405-496.
