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The Iodothyronine Selenodeiodinases Are Thioredoxin-fold Family Proteins Containing a Glycoside Hydrolase Clan GH-A-like Structure

Year: 2003
Type: article
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.
DOI: 10.1074/jbc.m305725200
Authors: 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
Institutions: Centre National de la Recherche Scientifique, Institut de minéralogie, de physique des matériaux et de cosmochimie, Université Paris Diderot, Brigham and Women's Hospital, Harvard University, HUN-REN Institute of Experimental Medicine, Hungarian Academy of Sciences, Sanofi (France)
Language: English
Field: Medicine
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1963784968
FWCI: 5.354
Cites: 41
Cited by: 140
Related to: 10