Structure and function of the DNA-binding domain of the glucocorticoid receptor and other members of the nuclear receptor supergene family

1993 ◽  
Vol 26 (12) ◽  
pp. 644-650 ◽  
Author(s):  
Torleif Haerd ◽  
Jan Aake Gustafsson
Keyword(s):  
Dna Binding ◽  
Glucocorticoid Receptor ◽  
Nuclear Receptor ◽  
Structure And Function ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
And Function ◽  
Supergene Family

scholarly journals Relationship of Structure and Function of DNA-Binding Domain in Vitamin D Receptor

Molecules ◽  
2015 ◽  
Vol 20 (7) ◽  
pp. 12389-12399 ◽  
Author(s):  
Lin-Yan Wan ◽  
Yan-Qiong Zhang ◽  
Meng-Di Chen ◽  
Chang-Bai Liu ◽  
Jiang-Feng Wu
Keyword(s):  
Vitamin D ◽  
Dna Binding ◽  
Vitamin D Receptor ◽  
Structure And Function ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
And Function ◽  
Relationship Of

scholarly journals Transactivation Functions of the N-Terminal Domains of Nuclear Hormone Receptors: Protein Folding and Coactivator Interactions

2003 ◽  
Vol 17 (1) ◽  
pp. 1-10 ◽  
Author(s):  
Raj Kumar ◽  
E. Brad Thompson
Keyword(s):  
Dna Binding ◽  
Protein Interactions ◽  
Hormone Receptors ◽  
Nuclear Hormone Receptor ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Protein Protein Interactions ◽  
Carboxy Terminal ◽  
And Function ◽  
Terminal Domains

Abstract The N-terminal domains (NTDs) of many members of the nuclear hormone receptor (NHR) family contain potent transcription-activating functions (AFs). Knowledge of the mechanisms of action of the NTD AFs has lagged, compared with that concerning other important domains of the NHRs. In part, this is because the NTD AFs appear to be unfolded when expressed as recombinant proteins. Recent studies have begun to shed light on the structure and function of the NTD AFs. Recombinant NTD AFs can be made to fold by application of certain osmolytes or when expressed in conjunction with a DNA-binding domain by binding that DNA-binding domain to a DNA response element. The sequence of the DNA binding site may affect the functional state of the AFs domain. If properly folded, NTD AFs can bind certain cofactors and primary transcription factors. Through these, and/or by direct interactions, the NTD AFs may interact with the AF2 domain in the ligand binding, carboxy-terminal portion of the NHRs. We propose models for the folding of the NTD AFs and their protein-protein interactions.

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