An intrinsically disordered transcription activation domain increases the DNA binding affinity and reduces the specificity of NFκB p50/RelA.

Baughman HER, Narang D, Chen W, Villagrán Suárez AC, Lee J, Bachochin MJ, Gunther TR, Wolynes PG, Komives EA, J Biol Chem :102349 (2022) Europe PMC

SASDHF5 – Rel Homology Domain of p50/RelA bound to Urokinase kB site DNA

NF-kappa-B p105 subunit 39-350
Transcription factor p65 19-321
Urokinase kB
MWexperimental 79 kDa
MWexpected 79 kDa
VPorod 244 nm3
log I(s) 4.36×101 4.36×100 4.36×10-1 4.36×10-2
NF-kappa-B p105 subunit 39-350 Transcription factor p65 19-321 Urokinase kB small angle scattering data  s, nm-1
ln I(s)
NF-kappa-B p105 subunit 39-350 Transcription factor p65 19-321 Urokinase kB Guinier plot ln 4.37×101 Rg: 4.1 nm 0 (4.1 nm)-2 s2
(sRg)2I(s)/I(0)
NF-kappa-B p105 subunit 39-350 Transcription factor p65 19-321 Urokinase kB Kratky plot 1.104 0 3 sRg
p(r)
NF-kappa-B p105 subunit 39-350 Transcription factor p65 19-321 Urokinase kB pair distance distribution function Rg: 4.3 nm 0 Dmax: 13 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of the Rel Homology Domain of p50/RelA bound to Urokinase kB site DNA in 25 mM Tris.Cl, 150 mM NaCl, 1 mM DTT, 0.5 mM EDTA, pH 7.5 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS; Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.127 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1.3 and 5 mg/ml were measured at 10°C. 50 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Storage temperature = UNKNOWN

NF-kappa-B p105 subunit 39-350 (Nfkb1)
Mol. type   Protein
Organism   Mus musculus
Olig. state   Monomer
Mon. MW   35.9 kDa
 
UniProt   P25799 (39-350)
Sequence   FASTA
 
Transcription factor p65 19-321 (Rela)
Mol. type   Protein
Organism   Mus musculus
Olig. state   Monomer
Mon. MW   34.8 kDa
 
UniProt   Q04207 (19-321)
Sequence   FASTA
 
Urokinase kB
Mol. type   DNA
Olig. state   Monomer
Mon. MW   8.3 kDa
Sequence   FASTA