NMR-derived secondary structure of the full-length Ox40 mRNA 3'UTR and its multivalent binding to the immunoregulatory RBP Roquin.

Tants JN, Becker LM, McNicoll F, Müller-McNicoll M, Schlundt A, Nucleic Acids Res (2022) Europe PMC

SASDNW5 – apo Roquin-1 (coreROQ) at 50 µM, including concentration series data at 100, 200, 300 µM

Roquin-1
MWexperimental 19 kDa
MWexpected 18 kDa
VPorod 35 nm3
log I(s) 1.10×10-2 1.10×10-3 1.10×10-4 1.10×10-5
Roquin-1 small angle scattering data  s, nm-1
ln I(s)
Roquin-1 Guinier plot ln 1.11×10-2 Rg: 1.9 nm 0 (1.9 nm)-2 s2
(sRg)2I(s)/I(0)
Roquin-1 Kratky plot 1.104 0 √3 sRg
Dmax: 7 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of apo Roquin-1 (coreROQ) at 50 µM, including concentration series data at 100, 200, 300 µM in 150 mM NaCl, 20 mM Tris, 2 mM TCEP, pH 7 were collected on the EMBL P12 beam line at the PETRA III storage ring (DESY; Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 0.88 mg/ml was measured at 20°C. 10 successive 0.145 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.

Possibly aggregated. Concentration series data are made available in the full entry zip archive.

Roquin-1 (coreROQ)
Mol. type   Protein
Organism   Mus musculus
Olig. state   Monomer
Mon. MW   17.8 kDa
 
UniProt   Q4VGL6 (171-326)
Sequence   FASTA