Forced unfolding of the fibronectin type III module reveals a tensile molecular recognition switch.

@article{Krammer1999ForcedUO,
  title={Forced unfolding of the fibronectin type III module reveals a tensile molecular recognition switch.},
  author={Andr{\'e} Krammer and Hui Meng Lu and Barry Isralewitz and Klaus Schulten and V. Vogel},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1999},
  volume={96 4},
  pages={1351-6}
}
The 10th type III module of fibronectin possesses a beta-sandwich structure consisting of seven beta-strands (A-G) that are arranged in two antiparallel sheets. It mediates cell adhesion to surfaces via its integrin binding motif, Arg78, Gly79, and Asp80 (RGD), which is placed at the apex of the loop connecting beta-strands F and G. Steered molecular dynamics simulations in which tension is applied to the protein's terminal ends reveal that the beta-strand G is the first to break away from the… CONTINUE READING

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