RGS1 + G alpha I

RGS1 + G alpha I

RGS1 + G alpha I: Human regulator of G-protein signalling 1 in complex with the activated state of G alpha I
PDB Code: 2GTP
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.
RGS1 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.
Stimulation of the immune system results in a complex, coordinated signalling process that prepares the body to respond to an infection and elliminated the infection. A major element of this process is the activation of the B-cells which produce the antibodies that target the pathogen for destruction. Within the B-cells several genes are up-regulated upon activation. RGS1 is one that is immediately activated. The GAP activity of RGS1 is directed against Gia and Gqa G-proteins with the result that the direction of B-cell migration is altered. RGS1 even alters the movement of B-cells within lymph nodes. Demonstration that RGS1 is also upregulated by bacterial lipopolysaccharides enhances the suggestion that RGS1 plays a key role in the signalling response of the immune system.
Here we present the crystal structure of RGS1 in complex with the activated state of G alpha I

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