Allosteric autoregulation of DNA binding via a DNA-mimicking protein domain: a biophysical study of ZNF410-DNA interaction using small angle X-ray scattering.

Kaur G, Ren R, Hammel M, Horton JR, Yang J, Cao Y, He C, Lan F, Lan X, Blobel GA, Blumenthal RM, Zhang X, Cheng X, Nucleic Acids Res (2023) Europe PMC

SASDQF5 – Zinc finger protein 410 (ZNF410 full length)

Zinc finger protein 410
MWexperimental 56 kDa
MWexpected 52 kDa
VPorod 108 nm3
log I(s) 8.17×100 8.17×10-1 8.17×10-2 8.17×10-3
Zinc finger protein 410 small angle scattering data  s, nm-1
ln I(s)
Zinc finger protein 410 Guinier plot ln 8.17×100 Rg: 3.6 nm 0 (3.6 nm)-2 s2
Zinc finger protein 410 Kratky plot 1.104 0 3 sRg
Zinc finger protein 410 pair distance distribution function Rg: 3.9 nm 0 Dmax: 12.3 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Zinc finger protein 410 BILBOMD model

log I(s)
 s, nm-1
Zinc finger protein 410 BILBOMD model

Synchrotron SAXS data from solutions of ZNF410 (full length) in 20 mM Tris, 250 mM NaCl, 0.1% v/v β-mercaptoethanol, 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 2.1 m and at a wavelength of λ = 0.1127 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 55.00 μl sample at 4 mg/ml was injected at a 0.50 ml/min flow rate onto a Shodex KW-800 series column at 20°C. 30 successive 3 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.

Zinc finger protein 410 (ZNF410)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   52.1 kDa
UniProt   Q86VK4 (1-478)
Sequence   FASTA