Conformational dynamics of a regulator of G-protein signaling protein reveals a mechanism of allosteric inhibition by a small molecule.

@article{Vashisth2013ConformationalDO,
  title={Conformational dynamics of a regulator of G-protein signaling protein reveals a mechanism of allosteric inhibition by a small molecule.},
  author={Harish Vashisth and Andrew J Storaska and Richard R. Neubig and Charles L. Brooks},
  journal={ACS chemical biology},
  year={2013},
  volume={8 12},
  pages={2778-84}
}
Regulators of G protein signaling (RGS) proteins are key players in regulating signaling via G protein-coupled receptors. RGS proteins directly bind to the Gα-subunits of activated heterotrimeric G-proteins, and accelerate the rate of GTP hydrolysis, thereby rapidly deactivating G-proteins. Using atomistic simulations and NMR spectroscopy, we have studied in molecular detail the mechanism of action of CCG-50014, a potent small molecule inhibitor of RGS4 that covalently binds to cysteine… CONTINUE READING

From This Paper

Topics from this paper.
12 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 12 extracted citations

Similar Papers

Loading similar papers…