Description
RGS17, also known as regulator of G-protein signaling 17, attenuates the signaling activity of G-proteins by binding to activated, GTP-bound G alpha subunits and acting as a GTPase activating protein (GAP), increasing the rate of conversion of the GTP to GDP. This hydrolysis allows the G alpha subunits to bind G beta/gamma subunit heterodimers, forming inactive G-protein heterotrimers, thereby terminating the signal. It plays an important role in termination of signalling by mu opioid receptors and development of tolerance to opioid analgesic drugs. Recombinant human RGS17 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography