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

SASDVJ7 – Third double-stranded RNA-binding domain of Human Double-stranded RNA-specific adenosine deaminase (ADAR1) (wild-type, residues 708-801, i.e. ADAR1-dsRBD3)

Third double-stranded RNA-binding domain of human ADAR1 (wild-type, residues 708-801, i.e. ADAR1-dsRBD3)
MWexperimental 24 kDa
MWexpected 25 kDa
VPorod 39 nm3
log I(s) 1.51×10-2 1.51×10-3 1.51×10-4 1.51×10-5
Third double-stranded RNA-binding domain of human ADAR1 (wild-type, residues 708-801, i.e. ADAR1-dsRBD3) small angle scattering data  s, nm-1
ln I(s)
Third double-stranded RNA-binding domain of human ADAR1 (wild-type, residues 708-801, i.e. ADAR1-dsRBD3) Guinier plot ln 1.51×10-2 Rg: 2.4 nm 0 (2.4 nm)-2 s2
(sRg)2I(s)/I(0)
Third double-stranded RNA-binding domain of human ADAR1 (wild-type, residues 708-801, i.e. ADAR1-dsRBD3) Kratky plot 1.104 0 3 sRg
p(r)
Third double-stranded RNA-binding domain of human ADAR1 (wild-type, residues 708-801, i.e. ADAR1-dsRBD3) pair distance distribution function Rg: 2.5 nm 0 Dmax: 9.1 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) (wild-type, residues 708-801, i.e. ADAR1-dsRBD3) in 20 mM Na-phosphate, 100 mM NaCl, 2 mM 2-mercaptoethanol, pH 7 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. 21 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 (wild-type, residues 708-801, i.e. ADAR1-dsRBD3) (ADAR1-dsRBD3)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   12.6 kDa
 
UniProt   P55265 (708-801)
Sequence   FASTA