Solution Behavior of the Intrinsically Disordered N-Terminal Domain of Retinoid X Receptor α in the Context of the Full-Length Protein

Belorusova A, Osz J, Petoukhov M, Peluso-Iltis C, Kieffer B, Svergun D, Rochel N, Biochemistry 55(12):1741-1748 (2016) DOI

SASDMY4 – Retinoic acid receptor RXR-alpha DNA binding domain (DBD) in complex with Ramp2

Ramp2 DNA
Retinoic acid receptor RXR-alpha
MWexperimental 30 kDa
MWexpected 30 kDa
log I(s) 3.90×101 3.90×100 3.90×10-1 3.90×10-2
Ramp2 DNA Retinoic acid receptor RXR-alpha small angle scattering data  s, nm-1
ln I(s)
Ramp2 DNA Retinoic acid receptor RXR-alpha Guinier plot ln 3.90×101 Rg: 1.9 nm 0 (1.9 nm)-2 s2
(sRg)2I(s)/I(0)
Ramp2 DNA Retinoic acid receptor RXR-alpha Kratky plot 1.104 0 3 sRg
p(r)
Ramp2 DNA Retinoic acid receptor RXR-alpha pair distance distribution function Rg: 1.9 nm 0 Dmax: 5.8 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Ramp2 DNA Retinoic acid receptor RXR-alpha CUSTOM IN-HOUSE model

Synchrotron SAXS data from solutions of Retinoic acid receptor RXR-alpha DNA binding domain (DBD) in complex with Ramp2 in 20 mM Tris, 50 mM NaCl, 50 mM KCl, 5% glycerol, 2 mM Chaps, and 5 mM DTT, pH 7.5 were collected on the EMBL X33 beam line at the DORIS III, DESY storage ring (Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 2.7 m and at a wavelength of λ = 0.15 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 0.50 mg/ml was measured at 10°C. Eight successive 15 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.

Storage temperature = UNKNOWN

Tags: X33
Ramp2 DNA (Ramp2)
Mol. type   DNA
Olig. state   Monomer
Mon. MW   10.5 kDa
Sequence   FASTA
 
Retinoic acid receptor RXR-alpha (RXR DBD)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   9.9 kDa
 
UniProt   P19793
Sequence   FASTA