Activation of CCR5 by chemokines involves an aromatic cluster between transmembrane helices 2 and 3.

@article{Govaerts2003ActivationOC,
  title={Activation of CCR5 by chemokines involves an aromatic cluster between transmembrane helices 2 and 3.},
  author={C{\'e}dric Govaerts and Antoine Bondue and Jean-Yves Springael and Mireia Olivella and Xavier Deup{\'i} and Emmanuel Le Poul and Shoshana J. Wodak and Marc Parmentier and Leonardo Pardo and C{\'e}dric Blanpain},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 3},
  pages={1892-903}
}
CCR5 is a G protein-coupled receptor responding to four natural agonists, the chemokines RANTES (regulated on activation normal T cell expressed and secreted), macrophage inflammatory protein (MIP)-1 alpha, MIP-1 beta, and monocyte chemotactic protein (MCP)-2, and is the main co-receptor for the macrophage-tropic human immunodeficiency virus strains. We have previously identified a structural motif in the second transmembrane helix of CCR5, which plays a crucial role in the mechanism of… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 26 extracted citations

References

Publications referenced by this paper.
Showing 1-2 of 2 references

An Aromatic Cluster in CCR5 Activation 1903 by on A ril 17

  • Y. Ri, J. A. Ballesteros, +4 authors T. A. Bargiello
  • 1999

An Aromatic Cluster in CCR5 Activation 1902 by on A ril 17, 2008 w w w .jb.org D ow nladed fom

  • M. C. Gershengorn
  • Mol. Pharmacol
  • 1998

Similar Papers

Loading similar papers…