Expression of the Rat α1 Thyroid Hormone Receptor Ligand Binding Domain in Escherichia coli and the Use of a Ligand-Induced Conformation Change as a Method for Its Purification to Homogeneity

1995 ◽  
Vol 6 (3) ◽  
pp. 363-370 ◽  
Author(s):  
J.W. Apriletti ◽  
J.D. Baxter ◽  
K.H. Lau ◽  
B.L. West
Keyword(s):  
Escherichia Coli ◽  
Thyroid Hormone ◽  
Ligand Binding ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Conformation Change ◽  
Receptor Ligand

scholarly journals Definition of the Surface in the Thyroid Hormone Receptor Ligand Binding Domain for Association as Homodimers and Heterodimers with Retinoid X Receptor

2001 ◽  
Vol 276 (18) ◽  
pp. 14987-14995 ◽  
Author(s):  
Ralff C. J. Ribeiro ◽  
Weijun Feng ◽  
Richard L. Wagner ◽  
Cláudia H. R. M. Costa ◽  
Alexandre C. Pereira ◽  
...  
Keyword(s):  
Thyroid Hormone ◽  
Ligand Binding ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Retinoid X Receptor ◽  
Receptor Ligand ◽  
Definition Of

scholarly journals The tau 4 activation domain of the thyroid hormone receptor is required for release of a putative corepressor(s) necessary for transcriptional silencing.

1995 ◽  
Vol 15 (1) ◽  
pp. 76-86 ◽  
Author(s):  
A Baniahmad ◽  
X Leng ◽  
T P Burris ◽  
S Y Tsai ◽  
M J Tsai ◽  
...  
Keyword(s):  
Amino Acids ◽  
Thyroid Hormone ◽  
Ligand Binding ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Activation Domain ◽  
C Terminus

The C terminus of nuclear hormone receptors is a complex structure that contains multiple functions. We are interested in the mechanism by which thyroid hormone converts its receptor from a transcriptional silencer to an activator of transcription. Both regulatory functions are localized in the ligand binding domain of this receptor superfamily member. In this study, we have identified and characterized several functional domains within the ligand binding domain of the human thyroid hormone receptor (TR beta) conferring transactivation. Interestingly, these domains are localized adjacent to hormone binding sites. One activation domain, designated tau 4, is only 17 amino acids in length and is localized at the extreme C terminus of TR. Deletion of six amino acids of tau 4 resulted in a receptor that could still bind hormone but acted as a constitutive silencer, indicating that tau 4 is required for both transactivation and relief of the silencing functions. In addition, we performed in vivo competition experiments, the results of which suggest that in the absence of tau 4 or hormone, TR is bound by a corepressor protein(s) and that one role of hormone is to release corepressor from the receptor. We propose a general model in which the role of hormone is to induce a conformational change in the receptor that subsequently affects the action of tau 4, leading to both relief of silencing and transcriptional activation.

Preliminary Crystallographic Studies of the Ligand-binding Domain of the Thyroid Hormone Receptor Complexed with Triiodothyronine

1994 ◽  
Vol 237 (2) ◽  
pp. 236-239 ◽  
Author(s):  
Mary E. McGrath ◽  
Richard L. Wagner ◽  
James W. Apriletti ◽  
Brian L. West ◽  
V. Ramalingam ◽  
...  
Keyword(s):  
Thyroid Hormone ◽  
Ligand Binding ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor ◽  
Binding Domain ◽  
Ligand Binding Domain
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