New structural insights into the control of the retinoic acid receptors RAR/RXR by DNA, ligands, and transcriptional coregulators.

Tambones I, Sagar A, Vankova P, Loginov D, Carivenc C, Rochel N, Bourguet W, Man P, Bernadó P, le Maire A, Nucleic Acids Res 53(18) (2025) Europe PMC

SASDXR2 – RAR/RXR heterodimer : BMS493 : IR0 element

Retinoic acid receptor alpha
BMS493 (RAR inverse agonist ligand)
Retinoid X receptor alpha
Inverted Repeat binding site with zero-base-pair spacing
MWexperimental 83 kDa
MWexpected 89 kDa
VPorod 121 nm3
log I(s) 2.70×10-2 2.70×10-3 2.70×10-4 2.70×10-5
Retinoic acid receptor alpha BMS493 (RAR inverse agonist ligand) Retinoid X receptor alpha Inverted Repeat binding site with zero-base-pair spacing small angle scattering data  s, nm-1
ln I(s)
Retinoic acid receptor alpha BMS493 (RAR inverse agonist ligand) Retinoid X receptor alpha Inverted Repeat binding site with zero-base-pair spacing Guinier plot ln 2.70×10-2 Rg: 3.9 nm 0 (3.9 nm)-2 s2
(sRg)2I(s)/I(0)
Retinoic acid receptor alpha BMS493 (RAR inverse agonist ligand) Retinoid X receptor alpha Inverted Repeat binding site with zero-base-pair spacing Kratky plot 1.104 0 3 sRg
p(r)
Retinoic acid receptor alpha BMS493 (RAR inverse agonist ligand) Retinoid X receptor alpha Inverted Repeat binding site with zero-base-pair spacing pair distance distribution function Rg: 3.9 nm 0 Dmax: 12.9 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of RAR/RXR heterodimer : BMS493 : IR0 element in 20 mM Tris HCl, 75 mM NaCl, 75 mM KCl, 2 mM CHAPS, 4 mM MgCl₂, 12 mM TCEP, pH 7.5 were collected on the SWING beam line at the SOLEIL storage ring (Saint-Aubin, France) using a Eiger 4M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.10332 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 50.00 μl sample at 10 mg/ml was injected at a 0.20 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 15°C. 990 successive 1.990 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Retinoic acid receptor alpha (RARα)
Mol. type   Protein
Organism   Mus musculus
Olig. state   Monomer
Mon. MW   39.2 kDa
 
UniProt   P11416 (82-421)
Sequence   FASTA
 
BMS493 (RAR inverse agonist ligand)
Mol. type   Other
Olig. state   Monomer
Mon. MW   0.4 kDa
Chemical formula
 
Retinoid X receptor alpha (RXRα)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   38.4 kDa
 
UniProt   P19793 (126-462)
Sequence   FASTA
 
Inverted Repeat binding site with zero-base-pair spacing (IR0)
Mol. type   DNA
Olig. state   Monomer
Mon. MW   11.1 kDa
Sequence   FASTA