RGS8 + Galphai3

RGS8 + Galphai3

RGS8 + Galphai3: Human regulator of G-protein signalling 8 in complex with Galphai3
PDB Code: 2ODE
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.
RGS8 is a member of the B/R4 subfamily of RGS proteins. All of these subfamily members have an N-terminal amphipathic helix which enhances the localisation of the protein to the membrane surface where it is ideally placed to interact with the G-proteins.
RGS8 modulates the activity of the G-protein coupled inward rectifying K+ channel Kir3.1/Kir3.2. It is the Gbg subunits that bind directly to GIRK, activating the channel. As described above, RGS8 does have a GAP activity through its RGS domain, resulting in deactivation of the GIRK channel however RGS8 also enhances channel activity which has been attributed to its N-terminal region. Explanations for this behaviour have been accounted for through the generation of macromolecular assemblies involving ion channels, G-proteins, GPCR and RGS proteins.
Here we present the crystal structure of part of the macromolecular assembly that of RGS8 in complex with the Galphai3 subunit.

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