Iodothyronine deiodinases (Dios) are selenoproteins involved in the regioselective removal of iodine from thyroid hormones (THs). Catalytic deiodination is essential to maintain TH homeostasis, and disruption can have detrimental effects. Halogen bonding (XB) to the selenium of the Sec residue in the active site has been proposed as a possible mechanism for iodine removal of thyroxine (T4). In addition, a flexible loop located near the active site may be important for substrate binding in the monomer. SymDock and Chimera were used to construct dimer structures from the stable monomer structures of Dio3 having the key loop conformation and the T4-Dio3 XB interaction. The results of molecular dynamics (MD) simulations are presented to show the effect of dimerization on the catalytic loop conformation and the T4 XB interactions.

Modeling of the dimer structure of iodothyronine deiodinase

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.