GPCR/G protein


All GPCRs share a common seven trans-membrane structure. GPCRs are associated with heterotrimeric G-proteins which are GTP-binding proteins made of alpha, beta, and gamma subunits. When a ligand binds to GPCR, it activates the attached G-protein, the GDP is replaced with GTP. The activated G-protein then dissociates into an alpha and a beta-gamma complex which activates downstream signaling pathways. These intracellular signaling pathways include cAMP/PKA, calcium/NFAT, phospholipase C, protein tyrosine kinases, MAP kinases, PI-3-kinase, nitric oxide/cGMP, Rho, and JAK/STAT.
GPCRs are one of the most important therapeutic targets for various diseases, over 30% of all modern medicinal drugs target this family. Aberrant GPCR functions are involved in pathological conditions such as neurological, immunological and hormonal disorders. A large number of GPCRs have been identified, but whose ligands are not known, are classified as orphan receptors.
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B5327 M871Summary: Selective galanin GAL2 receptor antagonist -
B5328 AR-M 1896Summary: Selective GAL2 agonist -
B5329 Bay 55-9837Summary: Selective VPAC2 receptor agonist -
B5330 BIM 187Summary: Bombesin/GRP receptor agonist -
B5331 BIM 189Summary: Bombesin antagonist -
B5352 [Des-octanoyl]-Ghrelin (rat)Summary: Non-acylated, major circulating isoform of ghrelin -
B5358 Gastrin I (human)Summary: selective CCK2 receptor agonist -
B5359 Apelin-17 (human, bovine)Summary: Endogenous apelin receptor agonist -
B5360 Galanin (porcine)Summary: Endogenous porcine galanin receptor agonist -
B5361 Neuropeptide W-23 (human)Summary: Endogenous peptide agonist of Neuropeptide B/Neuropeptide W receptors NPBW1 and NPBW2

