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

SASDVF7 – Third double-stranded RNA-binding domain of Human Double-stranded RNA-specific adenosine deaminase (ADAR1) (residues 688-817, i.e. dsRBD3-long)

Third double-stranded RNA-binding domain of human ADAR1 (residues 688-817, i.e. dsRBD3-long)
MWexperimental 31 kDa
MWexpected 29 kDa
VPorod 50 nm3
log I(s) 1.96×10-2 1.96×10-3 1.96×10-4 1.96×10-5
Third double-stranded RNA-binding domain of human ADAR1 (residues 688-817, i.e. dsRBD3-long) small angle scattering data  s, nm-1
ln I(s)
Third double-stranded RNA-binding domain of human ADAR1 (residues 688-817, i.e. dsRBD3-long) Guinier plot ln 1.96×10-2 Rg: 2.6 nm 0 (2.6 nm)-2 s2
(sRg)2I(s)/I(0)
Third double-stranded RNA-binding domain of human ADAR1 (residues 688-817, i.e. dsRBD3-long) Kratky plot 1.104 0 √3 sRg
p(r)
Third double-stranded RNA-binding domain of human ADAR1 (residues 688-817, i.e. dsRBD3-long) pair distance distribution function Rg: 2.6 nm 0 Dmax: 8.0 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 688-817, i.e. dsRBD3-long) 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. 15 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 688-817, i.e. dsRBD3-long) (dsRBD3-long)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   14.7 kDa
 
UniProt   P55265 (688-817)
Sequence   FASTA