GABAB Family Related Drug Discovery Products
Membrane proteins are the most successful class of therapeutic targets. Creative Biolabs has developed a comprehensive collection of membrane protein in vitro assays for drug discovery that cover most membrane protein targets.
Creative Biolabs has the assays you can rely on for high throughput screening, lead optimization, characterizing and discovering targets, and uncovering the complexity of disease pathways. We can offer membrane protein in vitro assay kits that save valuable laboratory time and is ideal 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.
GABAB1a/b and GABAB2 subunits combine to form the heterodimeric G protein-coupled receptor known as the GABAB receptor. The extracellular Venus flytrap (VFT) region of the GABAB1a/b subunit is where the endogenous orthosteric agonist GABA attaches. The receptor is an intriguing target for the development of new drugs because it is linked to a variety of neurological and neuropsychiatric problems, such as learning and memory impairments, depression and anxiety, addiction, and epilepsy.
Creative Biolabs can provide a wide variety of high-quality GABAB family assays and products to meet the needs of drug discovery:
Overview of GABAB Family
The GABAB1 and GABAB2 subunits combine to form the GABAB-R, an obligatory heterodimer. Studies modifying the receptor makeup and binding studies on isolated GABAB2 subunits revealed that the GABAB2 7TM domain is primarily in charge of enticing G-proteins in addition to housing an allosteric binding site. The GABAB1 7TM participates in the production of GABAB-R oligomers by interacting with other GABAB1 7TMs in the inactive state, according to biochemical and biophysical investigations. The GABAB1 subunit has several isoforms, but the two that are most prevalent are GABAB1a and GABAB1b, which are both encoded by the same gene, GABAB1. They only structurally differ in the N-terminal region, where there are two repeats of the so-called sushi domain. GABAB2 masks a retention signal that is present in the end of GABAB1's coiled-coil domain, therefore dimerization with GABAB2 is necessary for GABAB1 to be transported from the endoplasmic reticulum (ER) to the cell surface. Moreover, numerous proteins involved in the regulation of the receptor, such as the proteins that have a tetramerization domain in the potassium channel, bind to the C-terminal GABAB-R region.
Fig.1 Proposed structure of the GABAB heterodimer in active and inactive states. (Marshall & Foord, 2010)
GABAB Family Drug Discovery
Due to its involvement in a variety of disorders, the GABAB-R is regarded as a particularly intriguing therapeutic target. But only one substance is now being used in clinical settings. The therapeutic potential of GABAB-R drugs may grow with the discovery of allosteric modulators. The complete receptor's most recent cryo-EM structure, which offers new opportunities for drug discovery, reveals similarities to other class C GPCRs. For a complete understanding of the receptor-mediated mechanisms and pathophysiology, as well as for the development of new drugs with favorable pharmacokinetics for clinical use, further characterization and investigation of putative allosteric binding pockets, intracellular signaling pathways, and the development of new ligands are essential.
Reference
- Marshall, F.H., & Foord, S.M. Heterodimerization of the GABAB receptor—implications for GPCR signaling and drug discovery. Advances in pharmacology. 2010, 58: 63-91.
