Designed to be stable: Crystal structure of a consensus ankyrin repeat protein

@article{Kohl2003DesignedTB,
  title={Designed to be stable: Crystal structure of a consensus ankyrin repeat protein},
  author={Andreas Kohl and H. Kaspar Binz and Patrik Forrer and Michael T. Stumpp and Andreas Pl{\"u}ckthun and Markus G. Grütter},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2003},
  volume={100},
  pages={1700 - 1705}
}
  • A. Kohl, H. Binz, M. Grütter
  • Published 3 February 2003
  • Biology
  • Proceedings of the National Academy of Sciences of the United States of America
Ankyrin repeat (AR) proteins mediate innumerable protein–protein interactions in virtually all phyla. This finding suggested the use of AR proteins as designed binding molecules. Based on sequence and structural analyses, we designed a consensus AR with fixed framework and randomized interacting residues. We generated several combinatorial libraries of AR proteins consisting of defined numbers of this repeat. Randomly chosen library members are expressed in soluble form in the cytoplasm of… 

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