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

SASDF54 – RXRΔH12/RAR Heterodimer : N-CoRNID Complex (1:1)

Nuclear receptor CoRepressor 1; Nuclear Receptor Interaction Domain (NID)
Retinoid-X receptor alpha (RXR-alpha) Ligand Binding Domain (LBD)
Retinoid-X receptor alpha (RXR-alpha) Δ helix12
MWexperimental 79 kDa
MWexpected 79 kDa
VPorod 183 nm3
log I(s) 2.79×103 2.79×102 2.79×101 2.79×100
Nuclear receptor CoRepressor 1; Nuclear Receptor Interaction Domain (NID) Retinoid-X receptor alpha (RXR-alpha) Ligand Binding Domain (LBD) Retinoid-X receptor alpha (RXR-alpha) Δ helix12 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) Retinoid-X receptor alpha (RXR-alpha) Δ helix12 Guinier plot ln 2.79×103 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) Retinoid-X receptor alpha (RXR-alpha) Δ helix12 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) Retinoid-X receptor alpha (RXR-alpha) Δ helix12 pair distance distribution function Rg: 4.2 nm 0 Dmax: 15.7 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of RXRΔH12/RAR Heterodimer : N-CoRNID Complex (1:1) 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 0.8 and 11.2 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.

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
 
Retinoid-X receptor alpha (RXR-alpha) Δ helix12 (RXRΔH12)
Mol. type   Protein
Organism   Mus musculus
Olig. state   Monomer
Mon. MW   23.5 kDa
 
UniProt   P28700 (227-439)
Sequence   FASTA