Origins of DNA-binding specificity: role of protein contacts with the DNA backbone.

@article{Schildbach1999OriginsOD,
  title={Origins of DNA-binding specificity: role of protein contacts with the DNA backbone.},
  author={Joel F. Schildbach and A. Wali Karzai and Brigitte E. Raumann and Robert T. Sauer},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1999},
  volume={96 3},
  pages={
          811-7
        }
}
A central question in protein-DNA recognition is the origin of the specificity that permits binding to the correct site in the presence of excess, nonspecific DNA. In the P22 Arc repressor, the Phe-10 side chain is part of the hydrophobic core of the free protein but rotates out to pack against the sugar-phosphate backbone of the DNA in the repressor-operator complex. Characterization of a library of position 10 variants reveals that Phe is the only residue that results in fully active Arc. One… CONTINUE READING
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