Identification and characterization of a selenoprotein family containing a diselenide bond in a redox motif.

@article{Shchedrina2007IdentificationAC,
  title={Identification and characterization of a selenoprotein family containing a diselenide bond in a redox motif.},
  author={Valentina A Shchedrina and Sergey V. Novoselov and Mikalai Yu Malinouski and Vadim N. Gladyshev},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2007},
  volume={104 35},
  pages={13919-24}
}
Selenocysteine (Sec, U) insertion into proteins is directed by translational recoding of specific UGA codons located upstream of a stem-loop structure known as Sec insertion sequence (SECIS) element. Selenoproteins with known functions are oxidoreductases containing a single redox-active Sec in their active sites. In this work, we identified a family of selenoproteins, designated SelL, containing two Sec separated by two other residues to form a UxxU motif. SelL proteins show an unusual… CONTINUE READING
22 Citations
1 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 22 extracted citations

References

Publications referenced by this paper.

Selenium, Its Molecular Biology and Role in Human Health eds

  • AL Small-Howard, Berry, MJ
  • Hatfi eld, DL,
  • 2006

Similar Papers

Loading similar papers…