Substrate interactions between trypanothione reductase and N1-glutathionylspermidine disulphide at 0.28-nm resolution.

@article{Bailey1993SubstrateIB,
  title={Substrate interactions between trypanothione reductase and N1-glutathionylspermidine disulphide at 0.28-nm resolution.},
  author={Sasaneh Bailey and Kristina Smith and Alan H. Fairlamb and William N. Hunter},
  journal={European journal of biochemistry},
  year={1993},
  volume={213 1},
  pages={67-75}
}
The enzyme trypanothione reductase has been identified as a prime target for the rational design of inhibitors which may have clinical use in the treatment of tropical diseases caused by the genera Trypanosoma and Leishmania. To aid the design or identification of new inhibitors of this enzyme we have elucidated the structural detail of a trypanothione reductase complexed with one of the naturally occurring substrates, N1-glutathionylspermidine disulphide, by single-crystal X-ray diffraction… CONTINUE READING