Two perfectly conserved arginine residues are required for substrate binding in a high-affinity nitrate transporter.

@article{Unkles2004TwoPC,
  title={Two perfectly conserved arginine residues are required for substrate binding in a high-affinity nitrate transporter.},
  author={Shiela E. Unkles and Duncan A. Rouch and Ye Wang and Mohammad Siddiqi and Anthony D. M. Glass and James Robertson Kinghorn},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2004},
  volume={101 50},
  pages={17549-54}
}
This study represents the first attempt to investigate the molecular mechanisms by which nitrate, an anion of significant ecological, agricultural, and medical importance, is transported into cells by high-affinity nitrate transporters. Two charged residues, R87 and R368, located within hydrophobic transmembrane domains 2 and 8, respectively, are conserved in all 52 high-affinity nitrate transporters sequenced thus far. Site-directed replacements of either of R87 or R368 residues by lysine were… CONTINUE READING

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