Characterization of the Ligand-Binding Domain of the Ecdysteroid Receptor from Drosophila Melanogaster

2003 ◽  
Vol 384 (1) ◽  
Author(s):  
M. Grebe ◽  
S. Przibilla ◽  
V.C. Henrich ◽  
M. Spindler-Barth
Keyword(s):  
Drosophila Melanogaster ◽  
Ligand Binding ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Ecdysteroid Receptor

scholarly journals Systematic and functional characterization of novel androgen receptor variants arising from alternative splicing in the ligand-binding domain

Oncogene ◽  
2016 ◽  
Vol 36 (10) ◽  
pp. 1440-1450 ◽  
Author(s):  
T Uo ◽  
H Dvinge ◽  
C C Sprenger ◽  
R K Bradley ◽  
P S Nelson ◽  
...  
Keyword(s):  
Androgen Receptor ◽  
Alternative Splicing ◽  
Ligand Binding ◽  
Functional Characterization ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Androgen Receptor Variants

scholarly journals Characterization of the Nurr1 ligand-binding domain co-activator interaction surface

2006 ◽  
Vol 37 (2) ◽  
pp. 317-326 ◽  
Author(s):  
Nikolaos Volakakis ◽  
Michal Malewicz ◽  
Banafsheh Kadkhodai ◽  
Thomas Perlmann ◽  
Gerard Benoit
Keyword(s):  
Ligand Binding ◽  
Binding Site ◽  
Close Association ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Site Directed Mutagenesis ◽  
Orphan Nuclear Receptor ◽  
Hydrophobic Region ◽  
Binding Surface

The recently solved crystal structure of the orphan nuclear receptor (NR) Nurr1 ligand-binding domain (LBD) showed that Nurr1 lacks a cavity for ligand binding and a canonical NR co-activator-binding site. Computer modeling of the Nurr1 LBD structure identified a hydrophobic region on the surface of the Nurr1 LBD that was positioned on the opposite side from the classical co-activator-binding site. Site-directed mutagenesis demonstrated that this region is critical for the activity of the Nurr1 LBD. Most mutations introduced in this region reduced or abolished transcriptional activity of the Nurr1 LBD, but mutation at lysine (K577) resulted in a drastically increased activity. Moreover, the activity of the Nurr1 LBD was shown to correlate with a propensity for proteasome-dependent degradation revealing a close association between activity and Nurr1 protein turnover. These data provide novel insights into the mechanisms of transcription via the Nurr1 LBD and identify an alternative co-activator-binding surface that is unique to the NR4A family of NRs.

scholarly journals Equilibrium unfolding of the retinoid X receptor ligand binding domain and characterization of an unfolding intermediate

2009 ◽  
Vol 141 (1) ◽  
pp. 1-10 ◽  
Author(s):  
Mark E. Harder ◽  
Dean A. Malencik ◽  
Xuguang Yan ◽  
David Broderick ◽  
Mark Leid ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Retinoid X Receptor ◽  
Receptor Ligand ◽  
Equilibrium Unfolding

Identification and biochemical characterization of the ligand binding domain of the collagen adhesin from Staphylococcus aureus

Biochemistry ◽  
1993 ◽  
Vol 32 (42) ◽  
pp. 11428-11435 ◽  
Author(s):  
Joseph M. Patti ◽  
Jeffrey O. Boles ◽  
Magnus Hook
Keyword(s):  
Staphylococcus Aureus ◽  
Ligand Binding ◽  
Biochemical Characterization ◽  
Binding Domain ◽  
Ligand Binding Domain
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