RGS6: Human regulator of G-protein signalling 6
PDB Code: 2ES0
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 Gα and Gβγ subunits. In the inactive state Gα and Gβγ exist as a complex with the Gα GTPase in an inactive GDP bound state. Upon activation GDP is replaced with GTP which induces Gα and Gβγ complex disassociation. At this stage both Gα and Gβγ proteins are active. Gα 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 -Gα protein can recombine with Gβγ thus terminating the signal.
RGS 6 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.
The closest family member to RGS6 is RGS7 whose structure was also solved by us . The interesting observation betweeen the two crystal forms is that both structures dimerise via a domain swap process to reform two correctly folded RGS domains within the asymmetric unit of the crystal. In both cases the domain swap region is the same, indicating that potentially the RGS domains of RGS6 and RGS7 are more dynamic than other family members.

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