The DNA-binding domain of the hexameric arginine repressor.

@article{Grandori1995TheDD,
  title={The DNA-binding domain of the hexameric arginine repressor.},
  author={R Grandori and T A Lavoie and Michelle Pflumm and Guoling Tian and Helmut Niersbach and Werner K. Maas and Ronald Fairman and Jason Carey},
  journal={Journal of molecular biology},
  year={1995},
  volume={254 2},
  pages={150-62}
}
The arginine repressor of Escherichia coli is a classical feedback regulator, signalling the availability of L-arginine inside the cell. It differs from most other bacterial repressors in functioning as a hexamer, but structural details have been lacking and its shares no clear sequence homologies with other transcriptional regulators. Analysis of the amino acid residue sequence and proteolytic cleavage pattern of the repressor was used to identify a region predicted to house the DNA-binding… CONTINUE READING
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In Proteins, Amino Acids and Peptides as Ions and Dipolar Ions, pp. 370–377

  • E. J. Cohn, J. T. Edsall
  • Reinhold Publishing Corporation,
  • 1943
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