RGS2: Human regulator of G-protein signalling 2
PDB Code: 2AF0
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.
RGS2 is a member of the B/R4 subfamily of RGS proteins and was originally identified as a protein that was up regulated in blood mononuclear cells 2 hours after the addition of lectin and cycloheximide . 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.
RGS2 has been shown to be directly involved in control of blood pressure making it an exciting new pharmaceutical target for hypertension.
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