scholarly journals Identification of Sulfhydryl-modified Cysteine Residues in the Ligand Binding Pocket of Retinoic Acid Receptor β

1997 ◽  
Vol 272 (2) ◽  
pp. 746-753 ◽  
Author(s):  
Christopher L. Wolfgang ◽  
Zhen-ping Zhang ◽  
Jerome L. Gabriel ◽  
Ronald A. Pieringer ◽  
Kenneth J. Soprano ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Ligand Binding ◽  
Retinoic Acid Receptor ◽  
Binding Pocket ◽  
Cysteine Residues ◽  
Ligand Binding Pocket ◽  
Acid Receptor

scholarly journals Correction to ‘Evolutionary diversification of retinoic acid receptor ligand-binding pocket structure by molecular tinkering'

2016 ◽  
Vol 3 (12) ◽  
pp. 160895
Author(s):  
Julianan Gutierrez-Mazariegos ◽  
Eswar Kumar Nadendla ◽  
Romain A. Studer ◽  
Susana Alvarez ◽  
Angel R. de Lera ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Ligand Binding ◽  
Retinoic Acid Receptor ◽  
Binding Pocket ◽  
Receptor Ligand ◽  
Ligand Binding Pocket ◽  
Acid Receptor ◽  
Evolutionary Diversification

scholarly journals Serine 232 and Methionine 272 Define the Ligand Binding Pocket in Retinoic Acid Receptor Subtypes

1998 ◽  
Vol 273 (6) ◽  
pp. 3490-3495 ◽  
Author(s):  
Jacek Ostrowski ◽  
Thor Roalsvig ◽  
Laura Hammer ◽  
Anne Marinier ◽  
John E. Starrett ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Ligand Binding ◽  
Retinoic Acid Receptor ◽  
Binding Pocket ◽  
Receptor Subtypes ◽  
Ligand Binding Pocket ◽  
Acid Receptor

Expression of human all-trans-retinoic acid receptor β and its ligand-binding domain in Escherichia coli

1995 ◽  
Vol 308 (1) ◽  
pp. 353-359 ◽  
Author(s):  
M Berggren Söderlund ◽  
G Johannesson ◽  
G Fex
Keyword(s):  
Escherichia Coli ◽  
Retinoic Acid ◽  
Ligand Binding ◽  
Retinoic Acid Receptor ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Acid Receptor ◽  
Recombinant Receptors ◽  
Trans Retinoic Acid ◽  
All Trans Retinoic Acid

all-trans-Retinoic acid, one of the hormonally active derivatives of vitamin A, occurs physiologically in plasma at a concentration below 10 nmol/l. The methods currently used for its quantification are based on HPLC, need about 1 ml of serum, are relatively laborious and thus not well suited for mass analysis. The affinity and specificity of retinoic acid receptors for all-trans-retinoic acid encouraged us to express both the entire human retinoic acid receptor beta (RAR-beta) and two versions of its retinoic acid-binding domain in Escherichia coli in the hope that these recombinant proteins might be used as binders in a ligand-binding assay for all-trans-retinoic acid. The recombinant receptors, the whole receptor [RAR-beta-(V7-Q448)], corresponding to domains A-F, and the ligand-binding domain [RAR-beta-(E149-Q448)], corresponding to domains D-F, were expressed in the vector pET 3d/BL21 (DE3) as inclusion bodies, solubilized with guanidinium chloride, renatured and purified by ion-exchange chromatography. RAR-beta-(P193-Q448), corresponding to domains E-F, was expressed in the vector pET 3d/BL21(DE3)pLysS, and purified by reversed-phase chromatography. Under non-denaturing conditions, the expressed whole receptor [RAR-beta-(V7-Q448)] and the D-F construct (RAR-beta-(E149-Q448)] behaved chromatographically as monomeric proteins whereas the E-F construct [RAR-beta-(P193-Q448)] had a strong tendency to aggregate. RAR-beta-(V7-Q448) and RAR-beta-(E149-Q448) had similar Kd values for all-trans-retinoic acid (1.4 and 0.6 nmol/l respectively) whereas RAR-beta-(P193-Q448) bound all-trans-retinoic acid less avidly (Kd 9.6 nmol/l). 9-cis-Retinoic acid bound to RAR-beta-(E149-Q448) and RAR-beta-(V7-Q448) as avidly as all-trans-retinoic acid. Competition experiments showed weak or no binding of 4-oxo-all-trans-retinoic acid, 4-oxo-13-cis-retinoic acid, 13-cis-retinoic acid, acitretin and retinol by RAR-beta-(E149-Q448).

Structural Determinants of the Ligand-Binding Site of the Human Retinoic Acid Receptor .alpha.

Biochemistry ◽  
1995 ◽  
Vol 34 (16) ◽  
pp. 5477-5485 ◽  
Author(s):  
Bruno Lefebvre ◽  
Christophe Rachez ◽  
Pierre Formstecher ◽  
Philippe Lefebvre
Keyword(s):  
Retinoic Acid ◽  
Ligand Binding ◽  
Binding Site ◽  
Retinoic Acid Receptor ◽  
Ligand Binding Site ◽  
Retinoic Acid Receptor Alpha ◽  
Structural Determinants ◽  
Acid Receptor ◽  
Receptor Alpha

scholarly journals Location of Two Photoaffinity-Labeled Sites on the Ligand-Binding Domain of Retinoic Acid Receptor .ALPHA..

1996 ◽  
Vol 19 (5) ◽  
pp. 659-664 ◽  
Author(s):  
Toru SASAKI ◽  
Rumiko SHIMAZAWA ◽  
Takayuki SAWADA ◽  
Toru IIJIMA ◽  
Hiroshi FUKASAWA ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Ligand Binding ◽  
Retinoic Acid Receptor ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Retinoic Acid Receptor Alpha ◽  
Acid Receptor ◽  
Receptor Alpha

Critical Role of Tyrosine 277 in the Ligand-Binding and Transactivating Properties of Retinoic Acid Receptor α†

Biochemistry ◽  
2000 ◽  
Vol 39 (9) ◽  
pp. 2183-2192 ◽  
Author(s):  
Sandrine Mailfait ◽  
Denise Belaiche ◽  
Mostafa Kouach ◽  
Nathalie Dallery ◽  
Philippe Chavatte ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Ligand Binding ◽  
Retinoic Acid Receptor ◽  
Critical Role ◽  
Acid Receptor ◽  
Retinoic Acid Receptor Α

scholarly journals A Mollusk Retinoic Acid Receptor (RAR) Ortholog Sheds Light on the Evolution of Ligand Binding

Endocrinology ◽  
2014 ◽  
Vol 155 (11) ◽  
pp. 4275-4286 ◽  
Author(s):  
Juliana Gutierrez-Mazariegos ◽  
Eswar Kumar Nadendla ◽  
Daniela Lima ◽  
Keely Pierzchalski ◽  
Jace W. Jones ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Ligand Binding ◽  
Retinoic Acid Receptor ◽  
Acid Receptor
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