The crystal structures of Chikungunya and Venezuelan equine encephalitis virus nsP3 macro domains define a conserved adenosine binding pocket.

@article{Malet2009TheCS,
  title={The crystal structures of Chikungunya and Venezuelan equine encephalitis virus nsP3 macro domains define a conserved adenosine binding pocket.},
  author={H{\'e}l{\`e}ne Malet and Bruno Coutard and Sa{\"i}d Jamal and H{\'e}l{\`e}ne Dutartre and Nicolas Papageorgiou and Maarit Neuvonen and Tero E. Ahola and Naomi Forrester and Ernest Andrew Gould and Daniel Lafitte and François Ferron and Julien Lescar and Alexander E. Gorbalenya and Xavier de Lamballerie and Bruno Canard},
  journal={Journal of virology},
  year={2009},
  volume={83 13},
  pages={6534-45}
}
Macro domains (also called "X domains") constitute a protein module family present in all kingdoms of life, including viruses of the Coronaviridae and Togaviridae families. Crystal structures of the macro domain from the Chikungunya virus (an "Old World" alphavirus) and the Venezuelan equine encephalitis virus (a "New World" alphavirus) were determined at resolutions of 1.65 and 2.30 A, respectively. These domains are active as adenosine di-phosphoribose 1''-phosphate phosphatases. Both the… CONTINUE READING
32 Citations
52 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 32 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 52 references

Crystal structures of the X-domains of a group-1 and a group-3 coronavirus reveal that ADP-ribose binding may not be a conserved property

  • Y. Piotrowski, G. Hansen, A. L. Boomars-van der Zanden, E. J. Snijder, A. E. Gorbalenya, R. Hilgenfeld
  • Protein Sci
  • 2009

Similar Papers

Loading similar papers…