The core domain of RGS16 retains G-protein binding and GAP activity in vitro, but is not functional in vivo.

@article{Chen1998TheCD,
  title={The core domain of RGS16 retains G-protein binding and GAP activity in vitro, but is not functional in vivo.},
  author={C Chen and Stephany C Lin},
  journal={FEBS letters},
  year={1998},
  volume={422 3},
  pages={359-62}
}
The regulators of G-protein signaling (RGS) family members contain a conserved region, the RGS domain, and are GTPase-activating proteins for many members of G-protein alpha-subunits. We report here that the core domain of RGS16 is sufficient for in vitro biochemical functions as assayed by its G-protein binding affinity and its ability to stimulate GTP hydrolysis by G alpha(o) protein. RGS16 also requires, in addition to the RGS domain, the divergent N-terminus for its biological function in… CONTINUE READING

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