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 Morse Pruitt and David P. Siderovski and Channing J Der and John E 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… CONTINUE READING
Highly Influential
This paper has highly influenced 12 other papers. REVIEW HIGHLY INFLUENTIAL CITATIONS
44 Citations
41 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 44 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 41 references

Endocytic protein intersectinl regulates actin assembly via Cdc 42 and NWASP

  • N. K. Hussain
  • Nature Cell Biol .
  • 2001

Molecular basis for Rac 1 recognition by guanine nucleotide exchange factors

  • A. E. Karnoub
  • Nature Struct . Biol .
  • 2001

Quantitative analysis of the effect of phosphoinositide interactions on the function of Dbl family proteins

  • J. T. Snyder
  • J . Biol . Chem .
  • 2001

Similar Papers

Loading similar papers…