Structural and functional analysis of the anti-malarial drug target prolyl-tRNA synthetase

@article{Jain2014StructuralAF,
  title={Structural and functional analysis of the anti-malarial drug target prolyl-tRNA synthetase},
  author={Vitul Jain and Haruhisa Kikuchi and Yoshiteru Oshima and Amit Kumar Sharma and Manickam Yogavel},
  journal={Journal of Structural and Functional Genomics},
  year={2014},
  volume={15},
  pages={181-190}
}
Aminoacyl-tRNA synthetases (aaRSs) drive protein translation in cells and hence these are essential enzymes across life. Inhibition of these enzymes can halt growth of an organism by stalling protein translation. Therefore, small molecule targeting of aaRS active sites is an attractive avenue from the perspective of developing anti-infectives. Febrifugine and its derivatives like halofuginone (HF) are known to inhibit prolyl-tRNA synthetase of malaria parasite Plasmodium falciparum. Here, we… CONTINUE READING
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