Structural basis for exquisite specificity of affinity clamps, synthetic binding proteins generated through directed domain-interface evolution.

@article{Huang2009StructuralBF,
  title={Structural basis for exquisite specificity of affinity clamps, synthetic binding proteins generated through directed domain-interface evolution.},
  author={Jin Huang and Koki Makabe and Matthew Biancalana and Akiko Koide and Shohei Koide},
  journal={Journal of molecular biology},
  year={2009},
  volume={392 5},
  pages={1221-31}
}
We have established a new protein-engineering strategy termed "directed domain-interface evolution" that generates a binding site by linking two protein domains and then optimizing the interface between them. Using this strategy, we have generated synthetic two-domain "affinity clamps" using PDZ and fibronectin type III (FN3) domains as the building blocks. While these affinity clamps all had significantly higher affinity toward a target peptide than the underlying PDZ domain, two distinct… CONTINUE READING