Thermodynamically reengineering the listerial invasion complex InlA/E-cadherin.

@article{Wollert2007ThermodynamicallyRT,
  title={Thermodynamically reengineering the listerial invasion complex InlA/E-cadherin.},
  author={Thomas Wollert and Dirk W. Heinz and W D Schubert},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2007},
  volume={104 35},
  pages={13960-5}
}
Biological processes essentially all depend on the specific recognition between macromolecules and their interaction partners. Although many such interactions have been characterized both structurally and biophysically, the thermodynamic effects of small atomic changes remain poorly understood. Based on the crystal structure of the bacterial invasion protein internalin (InlA) of Listeria monocytogenes in complex with its human receptor E-cadherin (hEC1), we analyzed the interface to identify… CONTINUE READING

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