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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Structural Determinants of RhoA Binding and Nucleotide Exchange in Leukemia-associated Rho Guanine-Nucleotide Exchange Factor*
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Mechanistic Insights into Specificity, Activity, and Regulatory Elements of the Regulator of G-protein Signaling (RGS)-containing Rho-specific Guanine Nucleotide Exchange Factors (GEFs) p115, PDZ-RhoGEF (PRG), and Leukemia-associated RhoGEF (LARG)*
TLDR
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RhoGEF Specificity Mutants Implicate RhoA as a Target for Dbs Transforming Activity
TLDR
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