RGS7: Human regulator of G-protein signalling 7
PDB Code: 2A72
Regulators of G-protein signalling (RGS) are domains that terminate the signal emanating from G-protein coupled receptors (GPCR). When a GPCR binds a specific ligand a signal is generated that is transmitted to the G-proteins that consist of the Ga and Gbg subunits. In the inactive state Ga and Gbg exist as a complex with the Ga GTPase in an inactive GDP bound state. Upon activation GDP is replaced with GTP which induces Ga and Gbg complex disassociation. At this stage both Ga and Gbg proteins are active. Ga does have an intrinsic GTPase activity but this is greatly enhanced by the association with an RGS domain. Hence RGS proteins act as GTPase activating proteins (GAPs). Once GTP hydrolysis has taken place the GDP-Ga protein can recombine with Gbg thus terminating the signal.
RGS7 is a member of the C/R7 subfamily of RGS proteins. The proteins within this subfamily contain multiple domains besides the RGS domain. These domains, including DEP (Disheveled, Egl-10, Pleckstrin), GGL (G-protein Gamma subunit-Like) and R7H (R7 Homology) domains, provide extra functionality to this group of RGS containing proteins. In the brain, RGS7 has an overlapping expression distribution with RGS17 with higher levels in the cerebellum. This may have a bearing on their cellular function as both RGS7 and RGS17 are involved in acute tolerance to analgesia administration even though RGS7 and RGS17 are from different subfamilies. However the mechanism of mu-opoid receptor regulation is likely to differ as the GGL domain of RGS7 is involved while RGS17 lacks this domain.
Two molecules were found the crystal asymmetric unit however they were formed not from individual RGS7 domains but by a combination of two RGS7 domains via a domain swap process. This crystal structure suggests a possible folding pattern for RGS domains that involves first the synthesis of the entire RGS domain before folding of the N-terminal helices around the C-terminal section.

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