Identification of lysines within alpha 1-antichymotrypsin important for DNA binding. An unusual combination of DNA-binding elements.

@article{Naidoo1995IdentificationOL,
  title={Identification of lysines within alpha 1-antichymotrypsin important for DNA binding. An unusual combination of DNA-binding elements.},
  author={Nishen Naidoo and Barry S. Cooperman and Zhi Mei Wang and Xinyao Liu and Harvey Rubin},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 24},
  pages={14548-55}
}
The human serum serine protease inhibitor (serpin) alpha 1-antichymotrypsin (ACT) appears to be unique among serpins in its ability to bind to double-stranded DNA. Using site-directed mutagenesis and chemical modification, a tri-lysine sequence (residues 210-212) falling within a solvent exposed loop and the C-terminal peptide containing two lysines (residues 391 and 396) were shown to be important for DNA binding. Mutation of residues 210-212 from lysines to either glutamates or threonines… CONTINUE READING