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

SASDHG5 – Nuclear factor kB p50/RelA bound to IFN kB site DNA

Transcription factor p65 19-549
NF-kappa-B p105 subunit 39-350
IFN kB DNA
MWexperimental 106 kDa
MWexpected 103 kDa
VPorod 314 nm3
log I(s) 5.44×101 5.44×100 5.44×10-1 5.44×10-2
Transcription factor p65 19-549 NF-kappa-B p105 subunit 39-350 IFN kB DNA small angle scattering data  s, nm-1
ln I(s)
Transcription factor p65 19-549 NF-kappa-B p105 subunit 39-350 IFN kB DNA Guinier plot ln 5.44×101 Rg: 5.1 nm 0 (5.1 nm)-2 s2
(sRg)2I(s)/I(0)
Transcription factor p65 19-549 NF-kappa-B p105 subunit 39-350 IFN kB DNA Kratky plot 1.104 0 3 sRg
p(r)
Transcription factor p65 19-549 NF-kappa-B p105 subunit 39-350 IFN kB DNA pair distance distribution function Rg: 5.3 nm 0 Dmax: 18.9 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of the Nuclear factor kB p50/RelA bound to IFN 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). One solute concentration of 1.25 mg/ml was measured at 10°C. 32 successive 10 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

Transcription factor p65 19-549 (Rela)
Mol. type   Protein
Organism   Mus musculus
Olig. state   Monomer
Mon. MW   58.4 kDa
 
UniProt   Q04207 (19-549)
Sequence   FASTA
 
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
 
IFN kB DNA
Mol. type   DNA
Olig. state   Monomer
Mon. MW   8.3 kDa
Sequence   FASTA