Region-specific anti-thyroid hormone receptor (TR) antibodies detect changes in TR structure due to ligand-binding and dimerization.
Journal Article (Journal Article)
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.
Full Text
Duke Authors
Cited Authors
- Yen, PM; Sugawara, A; Forgione, M; Spanjaard, RA; Macchia, E; Cheng, SY; Chin, WW
Published Date
- November 1993
Published In
Volume / Issue
- 97 / 1-2
Start / End Page
- 93 - 99
PubMed ID
- 7511545
International Standard Serial Number (ISSN)
- 0303-7207
Digital Object Identifier (DOI)
- 10.1016/0303-7207(93)90214-5
Language
- eng
Conference Location
- Ireland