Interplay of Protein Disorder in Retinoic Acid Receptor Heterodimer and Its Corepressor Regulates Gene Expression.

Cordeiro TN, Sibille N, Germain P, Barthe P, Boulahtouf A, Allemand F, Bailly R, Vivat V, Ebel C, Barducci A, Bourguet W, le Maire A, Bernadó P, Structure (2019) Europe PMC

SASDF84 – RXR/RAR Heterodimer : N-CoRNID Complex (1:1) with RAR agonist (Am580)

Nuclear receptor CoRepressor 1; Nuclear Receptor Interaction Domain (NID)
Retinoid-X receptor alpha (RXR-alpha) Ligand Binding Domain (LBD)
Retinoic acid receptor alpha (RAR-alpha) Ligand binding domain (LDB)
MWI(0) 50 kDa
MWexpected 84 kDa
VPorod 131 nm3
log I(s) 5.11×101 5.11×100 5.11×10-1 5.11×10-2
Nuclear receptor CoRepressor 1; Nuclear Receptor Interaction Domain (NID) Retinoid-X receptor alpha (RXR-alpha) Ligand Binding Domain (LBD) Retinoic acid receptor alpha (RAR-alpha) Ligand binding domain (LDB) small angle scattering data  s, nm-1
ln I(s)
Nuclear receptor CoRepressor 1; Nuclear Receptor Interaction Domain (NID) Retinoid-X receptor alpha (RXR-alpha) Ligand Binding Domain (LBD) Retinoic acid receptor alpha (RAR-alpha) Ligand binding domain (LDB) Guinier plot ln 5.12×101 Rg: 4.2 nm 0 (4.2 nm)-2 s2
(sRg)2I(s)/I(0)
Nuclear receptor CoRepressor 1; Nuclear Receptor Interaction Domain (NID) Retinoid-X receptor alpha (RXR-alpha) Ligand Binding Domain (LBD) Retinoic acid receptor alpha (RAR-alpha) Ligand binding domain (LDB) Kratky plot 1.104 0 3 sRg
p(r)
Nuclear receptor CoRepressor 1; Nuclear Receptor Interaction Domain (NID) Retinoid-X receptor alpha (RXR-alpha) Ligand Binding Domain (LBD) Retinoic acid receptor alpha (RAR-alpha) Ligand binding domain (LDB) pair distance distribution function Rg: 4.3 nm 0 Dmax: 17.2 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of RXR/RAR Heterodimer : N-CoRNID Complex (1:1) with RAR agonist (Am580) in 50mM Tris HCl, 150mM NaCl, 2mM TCEP, pH 7.5 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.099 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.9 and 3.5 mg/ml were measured at 10°C. 10 successive 1 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Note: Am580 = 4-[(5,6,7,8-Tetrahydro-5,5,8,8- tetramethyl-2- naphthalenyl) carboxamido]benzoic acid

Nuclear receptor CoRepressor 1; Nuclear Receptor Interaction Domain (NID) (N-CoR-NID)
Mol. type   Protein
Organism   Mus musculus
Olig. state   Monomer
Mon. MW   29.1 kDa
 
UniProt   Q60974 (2059-2325)
Sequence   FASTA
 
Retinoid-X receptor alpha (RXR-alpha) Ligand Binding Domain (LBD) (RXR)
Mol. type   Protein
Organism   Mus musculus
Olig. state   Monomer
Mon. MW   26.5 kDa
 
UniProt   P28700 (230-467)
Sequence   FASTA
 
Retinoic acid receptor alpha (RAR-alpha) Ligand binding domain (LDB) (RAR)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   28.0 kDa
 
UniProt   P10276 (173-421)
Sequence   FASTA