Dimerization of ADAR1 modulates site-specificity of RNA editing

Mboukou A, Rajendra V, Messmer S, Mandl T, Catala M, Tisné C, Jantsch M, Barraud P, Nature Communications 15(1) (2024) DOI

SASDVG7 – Third double-stranded RNA-binding domain of Human Double-stranded RNA-specific adenosine deaminase (ADAR1) (residues 708-801, i.e. dsRBD3-mid)

Third double-stranded RNA-binding domain of human ADAR1 (residues 708-801, i.e. dsRBD3-mid)
MWexperimental 19 kDa
MWexpected 22 kDa
VPorod 27 nm3
log I(s) 1.26×10-2 1.26×10-3 1.26×10-4 1.26×10-5
Third double-stranded RNA-binding domain of human ADAR1 (residues 708-801, i.e. dsRBD3-mid) small angle scattering data  s, nm-1
ln I(s)
Third double-stranded RNA-binding domain of human ADAR1 (residues 708-801, i.e. dsRBD3-mid) Guinier plot ln 1.26×10-2 Rg: 2.0 nm 0 (2.0 nm)-2 s2
(sRg)2I(s)/I(0)
Third double-stranded RNA-binding domain of human ADAR1 (residues 708-801, i.e. dsRBD3-mid) Kratky plot 1.104 0 3 sRg
p(r)
Third double-stranded RNA-binding domain of human ADAR1 (residues 708-801, i.e. dsRBD3-mid) pair distance distribution function Rg: 2.0 nm 0 Dmax: 6.7 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Third double-stranded RNA-binding domain of Human Double-stranded RNA-specific adenosine deaminase (ADAR1) (residues 708-801, i.e. dsRBD3-mid) in 20 mM Na-HEPES, 55 mM KOAc, 10 mM NaCl, 1 mM TCEP, pH 7.3 were collected on the SWING beam line at the SOLEIL storage ring (Saint-Aubin, France) using a Eiger 4M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.1033 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.00 mg/ml was measured at 10°C. Seven successive 0.990 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.

Third double-stranded RNA-binding domain of human ADAR1 (residues 708-801, i.e. dsRBD3-mid) (dsRBD3-mid)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   10.8 kDa
 
UniProt   P55265 (708-801)
Sequence   FASTA