Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid

Nature ◽  
1995 ◽  
Vol 378 (6558) ◽  
pp. 681-689 ◽  
Author(s):  
Jean-Paul Renaud ◽  
Natacha Rochel ◽  
Marc Ruff ◽  
Valéria Vivat ◽  
Pierre Chambon ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Retinoic Acid ◽  
Ligand Binding ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Trans Retinoic Acid ◽  
All Trans Retinoic Acid

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).

Crystal structure of nerve growth factor in complex with the ligand-binding domain of the TrkA receptor

Nature ◽  
10.1038/43705 ◽  
1999 ◽  
Vol 401 (6749) ◽  
pp. 184-188 ◽  
Author(s):  
Christian Wiesmann ◽  
Mark H. Ultsch ◽  
Steven H. Bass ◽  
Abraham M. de Vos
Keyword(s):  
Crystal Structure ◽  
Nerve Growth Factor ◽  
Growth Factor ◽  
Ligand Binding ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Trka Receptor ◽  
Nerve Growth

scholarly journals Crystal structure of the ligand-binding domain of the promiscuous EphA4 receptor reveals two distinct conformations

2010 ◽  
Vol 399 (4) ◽  
pp. 555-559 ◽  
Author(s):  
Nikhil Singla ◽  
Yehuda Goldgur ◽  
Kai Xu ◽  
Sari Paavilainen ◽  
Dimitar B. Nikolov ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Ligand Binding ◽  
Binding Domain ◽  
Ligand Binding Domain

How well can molecular modelling predict the crystal structure: the case of the ligand-binding domain of glutamate receptors

2000 ◽  
Vol 21 (3) ◽  
pp. 87-92 ◽  
Author(s):  
Yoav Paas ◽  
Anne Devillers-Thiéry ◽  
Vivian I Teichberg ◽  
Jean-Pierre Changeux ◽  
Miriam Eisenstein
Keyword(s):  
Crystal Structure ◽  
Ligand Binding ◽  
Glutamate Receptors ◽  
Molecular Modelling ◽  
Binding Domain ◽  
Ligand Binding Domain
Sign in / Sign up

Export Citation Format

Share Document