In silico insights into the dimer structure and deiodinase activity of type III iodothyronine deiodinase from bioinformatics, molecular dynamics simulations, and QM/MM calculations.

ABSTRACT: The homodimeric family of iodothyronine deiodinases (Dios) regioselectively remove iodine from thyroid hormones. Currently, structural data has only been reported for the monomer of the mus type III thioredoxin (Trx) fold catalytic domain (Dio3^Trx), but the mode of dimerization has not yet been determined. Various groups have proposed dimer structures that are similar to the A-type and B-type dimerization modes of peroxiredoxins. Computational methods are used to compare the sequence of Dio3^Trx to related proteins known to form A-type and B-type dimers. Sequence analysis and in silico protein-protein docking methods suggest that Dio3^Trx is more consistent with proteins that adopt B-type dimerization. Molecular dynamics (MD) simulations of the

SUBMITTER: Marsan ES 

PROVIDER: S-EPMC9878935 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature