The iodothyronine selenodeiodinases are thioredoxin-fold family proteins containing a glycoside hydrolase clan GH-A-like structure

Isabelle Callebaut, Cyntia Curcio-Morelli, Jean P. Mornon, Balazs Gereben, Christoph Buettner, Stephen Huang, Bertrand Castro, Tatiana L. Fonseca, John W. Harney, P. Reed Larsen, Antonio C. Bianco

Research output: Contribution to journalArticle

101 Scopus citations

Abstract

The three iodothyronine selenodeiodinases catalyze the initiation and termination of thyroid hormone effects in vertebrates. Structural analyses of these proteins have been hindered by their integral membrane nature and the inefficient eukaryotic-specific pathway for selenoprotein synthesis. Hydrophobic cluster analysis used in combination with Position-specific Iterated BLAST reveals that their extramembrane portion belongs to the thioredoxin-fold superfamily for which experimental structure information exists. Moreover, a large deiodinase region imbedded in the thioredoxin fold shares strong similarities with the active site of iduronidase, a member of the clan GH-A-fold of glycoside hydrolases. This model can explain a number of results from previous mutagenesis analyses and permits new verifiable insights into the structural and functional properties of these enzymes.

Original languageEnglish (US)
Pages (from-to)36887-36896
Number of pages10
JournalJournal of Biological Chemistry
Volume278
Issue number38
DOIs
StatePublished - Sep 19 2003

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Callebaut, I., Curcio-Morelli, C., Mornon, J. P., Gereben, B., Buettner, C., Huang, S., Castro, B., Fonseca, T. L., Harney, J. W., Larsen, P. R., & Bianco, A. C. (2003). The iodothyronine selenodeiodinases are thioredoxin-fold family proteins containing a glycoside hydrolase clan GH-A-like structure. Journal of Biological Chemistry, 278(38), 36887-36896. https://doi.org/10.1074/jbc.M305725200