Structural analysis of TIFA: Insight into TIFA-dependent signal transduction in innate immunity.

Nakamura T, Hashikawa C, Okabe K, Yokote Y, Chirifu M, Toma-Fukai S, Nakamura N, Matsuo M, Kamikariya M, Okamoto Y, Gohda J, Akiyama T, Semba K, Ikemizu S, Otsuka M, Inoue JI, Yamagata Y, Sci Rep 10(1):5152 (2020) Europe PMC

SASDHS5 – Full-length Mouse TIFA dimer

TRAF-interacting protein with FHA domain-containing protein A
MWexperimental 49 kDa
MWexpected 45 kDa
VPorod 85 nm3
log I(s) 1.40×100 1.40×10-1 1.40×10-2 1.40×10-3
TRAF-interacting protein with FHA domain-containing protein A small angle scattering data  s, nm-1
ln I(s)
TRAF-interacting protein with FHA domain-containing protein A Guinier plot ln 1.40×100 Rg: 3.1 nm 0 (3.1 nm)-2 s2
(sRg)2I(s)/I(0)
TRAF-interacting protein with FHA domain-containing protein A Kratky plot 1.104 0 √3 sRg
p(r)
TRAF-interacting protein with FHA domain-containing protein A pair distance distribution function Rg: 3.3 nm 0 Dmax: 15.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
TRAF-interacting protein with FHA domain-containing protein A DAMFILT model
SAXS data from solutions of TRAF-interacting protein with FHA domain-containing protein A in 20 mM HEPES, 150 mM NaCl, 100 mM arginine, 5 % glycerol, 10 mM DTT, pH 8 were collected using a Rigaku BioSAXS-1000 instrument (Kumamoto University, Japan) equipped with a Pilatus 100K detector at a sample-detector distance of 0.5 m and at a wavelength of λ = 0.15418 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 10.00 mg/ml was measured at 20°C (3600 s). The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Storage temperature = UNKNOWN. Number of frames = UNKNOWN

TRAF-interacting protein with FHA domain-containing protein A (TIFA (His-tagged))
Mol. type   Protein
Organism   Mus musculus
Olig. state   Dimer
Mon. MW   22.6 kDa
 
UniProt   Q793I8 (1-184)
Sequence   FASTA