Structural analysis reveals how tetrameric tyrosine-phosphorylated STAT1 is targeted by the rabies virus P-protein

Sugiyama A, Minami M, Ugajin K, Inaba-Inoue S, Yabuno N, Takekawa Y, Xiaomei S, Takei S, Sasaki M, Nomai T, Jiang X, Kita S, Maenaka K, Hirose M, Yao M, Gooley P, Moseley G, Sugita Y, Ose T, Science Signaling 18(878) (2025) DOI

SASDUL4 – Signal transducer and activator of transcription 1-alpha/beta (STAT1)

Signal transducer and activator of transcription 1-alpha/beta
MWexperimental 349 kDa
MWexpected 349 kDa
VPorod 800 nm3
log I(s) 1.19×10-1 1.19×10-2 1.19×10-3 1.19×10-4
Signal transducer and activator of transcription 1-alpha/beta small angle scattering data  s, nm-1
ln I(s)
Signal transducer and activator of transcription 1-alpha/beta Guinier plot ln 1.19×10-1 Rg: 6.2 nm 0 (6.2 nm)-2 s2
(sRg)2I(s)/I(0)
Signal transducer and activator of transcription 1-alpha/beta Kratky plot 1.104 0 3 sRg
p(r)
Signal transducer and activator of transcription 1-alpha/beta pair distance distribution function Rg: 6.4 nm 0 Dmax: 21.2 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of STAT1 in 10 mM HEPES-NaOH, 150 mM NaCl, 3% glycerol, 2 mM DTT, pH 7.4 were collected on the BL-10C beam line at the Photon Factory High Energy Accelerator Research Organization (KEK; Tsukuba, Japan) using a Pilatus3 2M detector at a sample-detector distance of 2.1 m and at a wavelength of λ = 0.1 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 130.00 μl sample at 9.2 mg/ml was injected at a 0.05 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 25°C. 309 successive 20 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.

Signal transducer and activator of transcription 1-alpha/beta (STAT1)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Tetramer
Mon. MW   87.3 kDa
 
UniProt   P42224 (1-750)
Sequence   FASTA