Hormone activity of hydroxylated polybrominated diphenyl ethers on human thyroid receptor-beta: in vitro and in silico investigations.

ABSTRACT:

Background

Hydroxylated polybrominated diphenyl ethers (HO-PBDEs) may disrupt thyroid hormone status because of their structural similarity to thyroid hormone. However, the molecular mechanisms of interactions with thyroid hormone receptors (TRs) are not fully understood.

Objectives

We investigated the interactions between HO-PBDEs and TRbeta to identify critical structural features and physicochemical properties of HO-PBDEs related to their hormone activity, and to develop quantitative structure-activity relationship (QSAR) models for the thyroid hormone activity of HO-PBDEs.

Methods

We used the recombinant two-hybrid yeast assay to determine the hormone activities to TRbeta and molecular docking to model the ligand-receptor interaction in the binding site. Based on

SUBMITTER: Li F 

PROVIDER: S-EPMC2866673 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature