Structural basis for the selective activation of Rho GTPases by Dbl exchange factors

@article{Snyder2002StructuralBF,
  title={Structural basis for the selective activation of Rho GTPases by Dbl exchange factors},
  author={Jason T. Snyder and David K. Worthylake and Kent L. Rossman and Laurie Betts and Wendy M. Pruitt and D. Siderovski and Channing J. Der and John Sondek},
  journal={Nature Structural Biology},
  year={2002},
  volume={9},
  pages={468-475}
}
Activation of Rho-family GTPases involves the removal of bound GDP and the subsequent loading of GTP, all catalyzed by guanine nucleotide exchange factors (GEFs) of the Dbl-family. Despite high sequence conservation among Rho GTPases, Dbl proteins possess a wide spectrum of discriminatory potentials for Rho-family members. To rationalize this specificity, we have determined crystal structures of the conserved, catalytic fragments (Dbl and pleckstrin homology domains) of the exchange factors… 
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TLDR
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