Crystal structure of mammalian selenocysteine-dependent iodothyronine deiodinase suggests a peroxiredoxin-like catalytic mechanism.

@article{Schweizer2014CrystalSO,
  title={Crystal structure of mammalian selenocysteine-dependent iodothyronine deiodinase suggests a peroxiredoxin-like catalytic mechanism.},
  author={Ulrich Schweizer and Christine Schlicker and Doreen Braun and Josef Koehrle and Clemens Steegborn},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2014},
  volume={111 29},
  pages={10526-31}
}
Local levels of active thyroid hormone (3,3',5-triiodothyronine) are controlled by the action of activating and inactivating iodothyronine deiodinase enzymes. Deiodinases are selenocysteine-dependent membrane proteins catalyzing the reductive elimination of iodide from iodothyronines through a poorly understood mechanism. We solved the crystal structure of the catalytic domain of mouse deiodinase 3 (Dio3), which reveals a close structural similarity to atypical 2-Cys peroxiredoxin(s) (Prx). The… CONTINUE READING

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Crystal structures of a poplar thioredoxin peroxidase that exhibits the structure of glutathione peroxidases: Insights into redox-driven conformational changes

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