The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function.

@article{Aota1994TheSA,
  title={The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function.},
  author={Shin-ichi Aota and Motoyoshi Nomizu and Kenneth M Yamada},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 40},
  pages={24756-61}
}
Synergistic sites in the central cell-adhesive domain of fibronectin (FN) substantially enhance cell adhesion mediated by the alpha 5 beta 1 integrin receptor for fibronectin. We characterized a critical minimal sequence needed for synergistic activity using site-directed mutagenesis and homology scanning using intramolecular chimeras. The minimal cell-binding domain of FN consisting of the 9th and 10th type III FN repeat was expressed in an Escherichia coli expression system. This protein… CONTINUE READING
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