The Yersinia adhesin YadA binds to a collagenous triple-helical conformation but without sequence specificity.

@article{Leo2008TheYA,
  title={The Yersinia adhesin YadA binds to a collagenous triple-helical conformation but without sequence specificity.},
  author={Jack C Leo and Heli Elovaara and Barbara Brodsky and Mikael Skurnik and Adrian Goldman},
  journal={Protein engineering, design & selection : PEDS},
  year={2008},
  volume={21 8},
  pages={
          475-84
        }
}
The Yersinia adhesin A (YadA) is a collagen-binding trimeric autotransporter of Yersinia enterocolitica, an enteropathogen that causes a range of gastroenteric and systemic diseases, and YadA is essential for Y. enterocolitica virulence. Although previous studies suggest a specific binding site in collagen for YadA, we found that recombinant YadA binds to both major cyanogen bromide fragments of collagen type II and the collagen-like model peptide (Pro-Hyp-Gly)(10) [(POG)(10)]. To further… CONTINUE READING
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