Analysis of Ligand Binding and Protein Dynamics of Human Retinoid X Receptor Alpha Ligand-Binding Domain by Nuclear Magnetic Resonance†

Biochemistry ◽  
2006 ◽  
Vol 45 (6) ◽  
pp. 1629-1639 ◽  
Author(s):  
Jianyun Lu ◽  
David P. Cistola ◽  
Ellen Li
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Ligand Binding ◽  
Protein Dynamics ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Retinoid X Receptor ◽  
Receptor Alpha ◽  
Retinoid X Receptor Alpha ◽  
Nuclear Magnetic

scholarly journals Characterization of the ligand binding domain of human retinoid X receptor alpha expressed in Escherichia coli

1994 ◽  
Vol 269 (28) ◽  
pp. 18662-18667
Author(s):  
L. Cheng ◽  
A.W. Norris ◽  
B.F. Tate ◽  
M. Rosenberger ◽  
J.F. Grippo ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Ligand Binding ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Retinoid X Receptor ◽  
Receptor Alpha ◽  
Retinoid X Receptor Alpha

scholarly journals The effect of antagonists on the conformational exchange of the retinoid X receptor alpha ligand-binding domain

2009 ◽  
Vol 47 (12) ◽  
pp. 1071-1080 ◽  
Author(s):  
Jianyun Lu ◽  
Marcia I. Dawson ◽  
Qiong Ying Hu ◽  
Zebin Xia ◽  
Jesse D. Dambacher ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Retinoid X Receptor ◽  
Conformational Exchange ◽  
Receptor Alpha ◽  
Retinoid X Receptor Alpha

scholarly journals Heterodimeric interaction between retinoid X receptor alpha and orphan nuclear receptor OR1 reveals dimerization-induced activation as a novel mechanism of nuclear receptor activation.

1997 ◽  
Vol 17 (7) ◽  
pp. 3977-3986 ◽  
Author(s):  
F F Wiebel ◽  
J A Gustafsson
Keyword(s):  
Ligand Binding ◽  
Nuclear Receptors ◽  
Nuclear Receptor ◽  
Transcriptional Activation ◽  
Receptor Activation ◽  
Binding Domain ◽  
Retinoid X Receptor ◽  
Transcriptional Responses ◽  
Receptor Alpha ◽  
Retinoid X Receptor Alpha

OR1 is a member of the steroid/thyroid hormone nuclear receptor superfamily which has been described to mediate transcriptional responses to retinoids and oxysterols. On a DR4 response element, an OR1 heterodimer with the nuclear receptor retinoid X receptor alpha (RXR alpha) has been described to convey transcriptional activation in both the absence and presence of the RXR ligand 9-cis retinoic acid, the mechanisms of which have remained unclear. Here, we dissect the effects of RXR alpha and OR1 ligand-binding domain interaction on transcriptional regulation and the role of the respective carboxy-terminal activation domains (AF-2s) in the absence and presence of the RXR ligand, employing chimeras of the nuclear receptors containing the heterologous GAL4 DNA-binding domain as well as natural receptors. The results show that the interaction of the RXR and OR1 ligand-binding domains unleashes a transcription activation potential that is mainly dependent on the AF-2 of OR1, indicating that interaction with RXR activates OR1. This defines dimerization-induced activation as a novel function of heterodimeric interaction and mechanism of receptor activation not previously described for nuclear receptors. Moreover, we present evidence that activation of OR1 occurs by a conformational change induced upon heterodimerization with RXR.

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