Region-specific anti-thyroid hormone receptor (TR) antibodies detect changes in TR structure due to ligand-binding and dimerization

Paul M. Yen, Akira Sugawara, Marc Forgione, Remco A. Spanjaard, Enrico Macchia, Sheue Yann Cheng, William W. Chin

研究成果: Article査読

11 被引用数 (Scopus)

抄録

There are multiple factors that potentially can induce structural changes in DNA-bound thyroid hormone receptors (TRs) including protein-protein interactions, ligand-binding to TRs, and the thyroid hormone response element (TRE) sequence. We used a battery of anti-TR antibodies that recognize the amino-terminal, hinge, or carboxy-terminal regions of TRs to study changes in the epitope regions of in vitro translated TRs in electrophoretic mobility shift assays. We found that the carboxy-terminal and hinge region antibodies recognized TR homodimers but not TR/T3-receptor auxiliary protein or TR/retinoid X receptor heterodimers. The amino-terminal antibodies detected conformational changes due to ligand binding. In contrast, each antibody recognized TR complexes bound to TREs containing half-sites arranged in three different orientations. These results suggest that dimerization with nuclear proteins and ligand-binding, rather than the orientation of TRE half-sites, cause changes in several TR subregions.

本文言語English
ページ(範囲)93-99
ページ数7
ジャーナルMolecular and Cellular Endocrinology
97
1-2
DOI
出版ステータスPublished - 1993 11月
外部発表はい

ASJC Scopus subject areas

  • 生化学
  • 分子生物学
  • 内分泌学

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