RGS2 + G alpha i3
RGS2 + G alpha i3: Human G-protein alpha (GNAI3) + with regulator of G-prot. signaling type 2 domain (RGS2)
PDB Code: 2V4Z
Regulators of G protein signalling (RGS) are multi functional GTPase activating protein (GAP) proteins for heterotrimeric G protein alpha subunits terminating the signals emanating from the G-Protein coupled receptors, which function as guanine nucleotide exchange factors (GEF) for the GTPase. RGS2 have been shown to function as a GAP for Gq class of G alpha proteins regulating its down stream signalling.
Recent expression studies and gene knock outs have identified RGS2 as a candidate gene for flt3-ITD mutations in acute myeloid leukemia (AML), anxiety disorder, blood pressure regulation, Bartter/Gitelman (BG) syndrome. RGS2 is implicated in T cell activation, synaptic development and basal electrical activity in hippocampal neurons and belongs to the R4 subfamily of RGS which mainly contain the conserved N-terminal RGS domain involved in plasma membrane localisation. This GAP protein expression is widely detected in all human tissues and have been suggested to play a regulatory role in GPCR mediated responses in the immune system, brain, heart, lungs and olfactory epithelium. The RGS2 -/- knockout mice revealed loss of blood pressure control resulting in profound hypertension with increased renal and systemic vascular resistance and hypertrophy of the renal vasculature.
RGS2 have been shown to interact preferentially with Gq but not with the Gαi isoforms. The basis of specificity between the heterotrimeric GTPase and the RGS proteins interactions is not understood. Here we present the crystal structure of engineered RGS2 molecule in complex with Gαi3 that binds to this GAP with high affinity. The structure gives insight into the molecular mechanism that defines GAP selectivity.
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