RGS10 (NMR)

RGS10 (NMR)

RGS10 (NMR): Human regulator of G-protein signalling 10
PDB Code: 2I59
Description
Regulators of G-protein signalling (RGS) proteins contain 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 Gα and Gβγ subunits. In the inactive state, Gα and Gβγ exist as a complex with the Gα GTPase in the inactive GDP bound form. 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.
RGS10 is a member of the D/R12 subfamily of RGS proteins. Unlike the R4 subfamily, RGS10 does not have an amphipathic helix at the N-terminus which for the R4 family members enhances the localisation of the protein to the membrane surface where it is ideally placed to interact with the G-proteins. Instead RGS10 is localised to the membrane surface by palmitylation of a conserved cysteine residue located in the RGS domain.
Phosphorylation of RGS10 by protein kinase C alpha causes its translocation to the nucleus with the result that its Galpha GAP activity is regulated through spatial reorganisation.
Here we present the crystal structure of RGS10 in complex with the activated state of Galphai3 plus the structure of the free form of the RGS10 box determined by NMR.
OBS.: Palmitoylation/palmitylation is a post-translational modification that consists of the addition of a 16 carbon fatty acid, palmitate, to a cysteine residue through the creation of a thioester link. Unlike other lipid modifications such as myristoylation and prenylation, which are irreversible, palmitoylation is a dynamic modification involving palmitoylation/depalmitoylation cycles suggesting a regulatory role. This is a common modification for mebrane proteins.

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