Crystal structural analysis of protein-protein interactions drastically destabilized by a single mutation.

@article{Urakubo2008CrystalSA,
  title={Crystal structural analysis of protein-protein interactions drastically destabilized by a single mutation.},
  author={Yoshiaki Urakubo and Teikichi Ikura and Nobutoshi Ito},
  journal={Protein science : a publication of the Protein Society},
  year={2008},
  volume={17 6},
  pages={1055-65}
}
The complex of barnase (bn) and barstar (bs), which has been widely studied as a model for quantitative analysis of protein-protein interactions, is significantly destabilized by a single mutation, namely, bs Asp39 --> Ala, which corresponds to a change of 7.7 kcal x mol(-1) in the free energy of binding. However, there has been no structural information available to explain such a drastic destabilization. In the present study, we determined the structure of the mutant complex at 1.58 A… CONTINUE READING
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