scholarly journals The solution structure of the human retinoic acid receptor-β DNA-binding domain

1993 ◽  
Vol 3 (1) ◽  
pp. 1-17 ◽  
Author(s):  
R. M. A. Knegtel ◽  
M. Katahira ◽  
J. G. Schilthuis ◽  
A. M. J. J. Bonvin ◽  
R. Boelens ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Dna Binding ◽  
Solution Structure ◽  
Retinoic Acid Receptor ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Acid Receptor

Production and characterization of a retinoic acid receptor RARγ construction encompassing the DNA binding domain and the disordered N-terminal proline rich domain

2014 ◽  
Vol 95 ◽  
pp. 113-120 ◽  
Author(s):  
Denise Martinez-Zapien ◽  
Marc-André Delsuc ◽  
Gilles Travé ◽  
Régis Lutzing ◽  
Cécile Rochette-Egly ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Dna Binding ◽  
Retinoic Acid Receptor ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Acid Receptor ◽  
Rich Domain

Heteronuclear 113Cd-1H NMR Study of Metal Coordination in the Human Retinoic Acid Receptor-β DNA Binding Domain

1993 ◽  
Vol 192 (2) ◽  
pp. 492-498 ◽  
Author(s):  
R.M.A. Knegtel ◽  
R. Boelens ◽  
M.L. Ganadu ◽  
A.V.E. George ◽  
P.T. Vandersaag ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Dna Binding ◽  
1H Nmr ◽  
Retinoic Acid Receptor ◽  
Binding Domain ◽  
Metal Coordination ◽  
Dna Binding Domain ◽  
Acid Receptor ◽  
Nmr Study

NMR Studies of the Human Retinoic Acid Receptor-? DNA-Binding Domain.

1993 ◽  
Vol 684 (1 Zinc-Finger P) ◽  
pp. 49-62 ◽  
Author(s):  
R. M. A. KNEGTEL ◽  
R. BOELENS ◽  
M. L. GANADU ◽  
A. V. E. GEORGE ◽  
M. KATAHIRA ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Dna Binding ◽  
Retinoic Acid Receptor ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Nmr Studies ◽  
Acid Receptor

Letter to Editor: Solution structure of the HPV-16 E2 DNA binding domain, a transcriptional regulator with a dimeric β-barrel fold

2004 ◽  
Vol 30 (2) ◽  
pp. 211-214 ◽  
Author(s):  
Alejandro D. Nadra ◽  
Tommaso Eliseo ◽  
Yu-Keung Mok ◽  
Fabio C.L. Almeida ◽  
Mark Bycroft ◽  
...  
Keyword(s):  
Dna Binding ◽  
Solution Structure ◽  
Transcriptional Regulator ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Hpv 16

scholarly journals Solution Structure of the DNA-Binding Domain of the Tomato Heat-Stress Transcription Factor HSF24

1996 ◽  
Vol 236 (3) ◽  
pp. 911-921 ◽  
Author(s):  
Jurgen Schultheiss ◽  
Olaf Kunert ◽  
Uwe Gase ◽  
Klaus-Dieter Scharf ◽  
Lutz Nover ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Heat Stress ◽  
Dna Binding ◽  
Solution Structure ◽  
Binding Domain ◽  
Dna Binding Domain

scholarly journals Characterization and purification of human retinoic acid receptor-γ 1 overexpressed in the baculovirus-insect cell system

1992 ◽  
Vol 287 (3) ◽  
pp. 833-840 ◽  
Author(s):  
A P Reddy ◽  
J Y Chen ◽  
T Zacharewski ◽  
H Gronemeyer ◽  
J J Voorhees ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Dna Binding ◽  
Mammalian Cells ◽  
Retinoic Acid Receptor ◽  
Expression System ◽  
Gel Filtration ◽  
Recombinant Baculovirus ◽  
Sf9 Cells ◽  
Acid Receptor ◽  
Gel Retardation

The full-length cDNA for the human retinoic acid receptor-gamma 1 (RAR-gamma 1) has been expressed to high levels in Spodoptera frugiferda (Sf9) cells using the baculovirus expression system. Western blot analysis revealed that RAR-gamma 1 expression increased between 32 and 60 h post-infection. The recombinant receptor was expressed primarily as a nuclear protein and displayed a molecular mass of 50 kDa as determined by SDS/PAGE and gel-filtration chromatography, consistent with its cDNA-deduced size. Based on ligand binding, 2 x 10(6) RAR-gamma 1 molecules were expressed per Sf9 cell, a level approx. 2000 times greater than in mammalian cells. The receptor was partially purified 300-fold by sequential anion-exchange, gel-filtration and DNA affinity chromatographies. The overexpressed receptor specifically bound all-trans-retinoic acid (RA) and the synthetic retinoid CD367 with high affinity (Kd 0.15 nM and 0.23 nM respectively). The RA metabolites 4-hydroxy-RA and 4-oxo-RA were poor competitors for [3H]CD367 binding to recombinant RAR-gamma 1 (K(i) > 1 microM), indicating that 4-oxidation of RA greatly reduces its affinity for RAR-gamma 1. Gel-retardation analysis demonstrated that RAR-gamma 1 specifically bound the RA response element of the mouse RAR-beta gene. RAR-gamma 1 species expressed from recombinant baculovirus (in Sf9 cells) and vaccinia virus (in HeLa cells) exhibited similar affinities for RA and CD367 and had comparable DNA-binding properties in gel-retardation experiments. Moreover, a similar requirement for additional DNA-binding stimulatory factor(s) was observed in both cases. These results provide a basis for the use of baculovirus-expressed RAR-gamma 1 in further functional and structural studies.

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