Integrative structural analysis of NF45-NF90 heterodimers reveals architectural rearrangements and oligomerization on binding dsRNA.

Winterbourne S, Jayachandran U, Zou J, Rappsilber J, Granneman S, Cook AG, Nucleic Acids Res 53(6) (2025) Europe PMC

SASDUB5 – Heterodimer complex of domain-associated zinc finger domains of Interleukin enhancer-binding factor 2 (29-390) and Interleukin enhancer-binding factor 3 (1-381)

Interleukin enhancer-binding factor 3
Interleukin enhancer-binding factor 2
MWexperimental 80 kDa
MWexpected 83 kDa
VPorod 127 nm3
log I(s) 1.19×10-1 1.19×10-2 1.19×10-3 1.19×10-4
Interleukin enhancer-binding factor 3 Interleukin enhancer-binding factor 2 small angle scattering data  s, nm-1
ln I(s)
Interleukin enhancer-binding factor 3 Interleukin enhancer-binding factor 2 Guinier plot ln 1.19×10-1 Rg: 3.5 nm 0 (3.5 nm)-2 s2
(sRg)2I(s)/I(0)
Interleukin enhancer-binding factor 3 Interleukin enhancer-binding factor 2 Kratky plot 1.104 0 3 sRg
p(r)
Interleukin enhancer-binding factor 3 Interleukin enhancer-binding factor 2 pair distance distribution function Rg: 3.6 nm 0 Dmax: 12.6 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Interleukin enhancer-binding factor 3 Interleukin enhancer-binding factor 2 GASBOR model

Synchrotron SAXS data from solutions of Heterodimer complex of domain-associated zinc finger domains of Interleukin enhancer-binding factor 2 (29-390) and Interleukin enhancer-binding factor 3 (1-381) in 20 mM HEPES, 150 mM NaCl, 1 mM DTT, pH 7.5 were collected on the B21 beam line at the Diamond Light Source storage ring (Didcot, UK) using a Eiger 4M detector at a sample-detector distance of 3.7 m and at a wavelength of λ = 0.0954 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 60.00 μl sample at 10 mg/ml was injected at a 0.10 ml/min flow rate onto a Cytiva Superdex 200 Increase 3.2/300 column at 15°C. 915 successive 0.005 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.

Interleukin enhancer-binding factor 3 (ILF3 DZF)
Mol. type   Protein
Organism   Mus musculus
Olig. state   Monomer
Mon. MW   42.5 kDa
 
UniProt   Q9Z1X4 (1-381)
Sequence   FASTA
 
Interleukin enhancer-binding factor 2 (ILF2 DZF)
Mol. type   Protein
Organism   Mus musculus
Olig. state   Monomer
Mon. MW   40.3 kDa
 
UniProt   Q9CXY6 (29-390)
Sequence   FASTA