Structural mimicry for vinculin activation by IpaA, a virulence factor of Shigella flexneri.

  title={Structural mimicry for vinculin activation by IpaA, a virulence factor of Shigella flexneri.},
  author={Cyril Hamiaux and Andr{\'e} van Eerde and Claude Parsot and Jaap Broos and Bauke W Dijkstra},
  journal={EMBO reports},
  volume={7 8},
Invasion of epithelial cells by Shigella flexneri is characterized by cytoskeletal rearrangements of the host cell membrane, promoting internalization of the bacterium. The bacterial effector IpaA is injected into the epithelial cell by a type III secretion apparatus and recruits vinculin to regulate actin polymerization at the site of entry. We analysed the complex formed between a carboxy-terminal fragment of IpaA (IpaA(560-633)) and the vinculin D1 domain (VD1), both in crystals and in… CONTINUE READING
12 Citations
31 References
Similar Papers


Publications citing this paper.
Showing 1-10 of 12 extracted citations


Publications referenced by this paper.
Showing 1-10 of 31 references

Structural and dynamic characterization of a vinculin binding site in the talin rod

  • T Izard, C Vonrhein
  • Biochemistry
  • 2006

The activity of the vinculin binding sites in talin is influenced by the stability of the helical bundles that make up the talin rod

  • BC Patel
  • J Biol Chem
  • 2006

The integration of macromolecular diffraction data

  • AG Leslie
  • Acta Crystallogr D
  • 2006
1 Excerpt

Similar Papers

Loading similar papers…