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

SASDN26 – apo Roquin-1 (Nterm B-site mut ROQ) at 50 µM, including concentration series data at 100, 300 µM

Roquin-1 Nterm Bmut (R135E, K136E, D322A, K323A)
MWexperimental 58 kDa
MWexpected 51 kDa
VPorod 92 nm3
log I(s) 4.27×10-2 4.27×10-3 4.27×10-4 4.27×10-5
Roquin-1 Nterm Bmut (R135E, K136E, D322A, K323A) small angle scattering data  s, nm-1
ln I(s)
Roquin-1 Nterm Bmut (R135E, K136E, D322A, K323A) Guinier plot ln 4.27×10-2 Rg: 3.5 nm 0 (3.5 nm)-2 s2
(sRg)2I(s)/I(0)
Roquin-1 Nterm Bmut (R135E, K136E, D322A, K323A) Kratky plot 1.104 0 3 sRg
Dmax: 15 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of apo Roquin-1 (Nterm B-site mut ROQ) at 50 µM, including concentration series data at 100, 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 (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 2.50 mg/ml was measured at 20.1°C. Nine 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 Nterm Bmut (R135E, K136E, D322A, K323A) (ROQ Nterm Bmut)
Mol. type   Protein
Organism   Mus musculus
Olig. state   Monomer
Mon. MW   51.0 kDa
 
UniProt   Q4VGL6 (1-454)
Sequence   FASTA