Structure of the cell-adhesion fragment of intimin from enteropathogenic Escherichia coli

@article{Kelly1999StructureOT,
  title={Structure of the cell-adhesion fragment of intimin from enteropathogenic Escherichia coli},
  author={Geoff P. Kelly and Sunil Prasannan and Sarah J Daniell and Keiran Fleming and Gad Frankel and Gordon Dougan and Ian F Connerton and Stephen Matthews},
  journal={Nature Structural Biology},
  year={1999},
  volume={6},
  pages={313-318}
}
Enteropathogenic Escherichia coli (EPEC) induce gross cytoskeletal rearrangement within epithelial cells, immediately beneath the attached bacterium. The C-terminal 280 amino acid residues of intimin (Int280; 30.1 kDa), a bacterial cell-adhesion molecule, mediate the intimate bacterial host–cell interaction. Recently, interest in this process has been stimulated by the discovery that the bacterial intimin receptor protein (Tir) is translocated into the host cell membrane, phosphorylated, and… CONTINUE READING

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X-PLOR manual version 3.1 (Yale University, New Haven, 318 nature structural biology

  • A. T. Brünger
  • 1999