Structural Description of the Nipah Virus Phosphoprotein and Its Interaction with STAT1.

Jensen MR, Yabukarski F, Communie G, Condamine E, Mas C, Volchkova V, Tarbouriech N, Bourhis JM, Volchkov V, Blackledge M, Jamin M, Biophys J (2020) Europe PMC

SASDHT4 – Phosphoprotein from Nipah virus

Phosphoprotein
MWI(0) 432 kDa
MWexpected 317 kDa
log I(s) 3.72×102 3.72×101 3.72×100 3.72×10-1
Phosphoprotein small angle scattering data  s, nm-1
ln I(s)
Phosphoprotein Guinier plot ln 3.73×102 Rg: 10.9 nm 0 (10.9 nm)-2 s2
(sRg)2I(s)/I(0)
Phosphoprotein Kratky plot 1.104 0 √3 sRg
p(r)
Phosphoprotein pair distance distribution function Rg: 11.2 nm 0 Dmax: 39.3 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of phosphoprotein in 20 mM Tris-HCL 150 mM NaCl, pH 7.5 were collected on the ID14-3 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.4 m and at a wavelength of λ = 0.931 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.80 mg/ml was measured at 4°C. 10 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.

Phosphoprotein
Mol. type   Protein
Organism   Nipah henipavirus
Olig. state   Tetramer
Mon. MW   79.4 kDa
 
UniProt   Q9IK91 (1-709)
Sequence   FASTA