Structural Basis for Antigen Recognition by Transglutaminase 2-specific Autoantibodies in Celiac Disease.

Chen X, Hnida K, Graewert MA, Andersen JT, Iversen R, Tuukkanen A, Svergun D, Sollid LM, J Biol Chem 290(35):21365-75 (2015) Europe PMC

SASDA38 – transglutaminase-2 (TGA2)

transglutaminase 2
MWI(0) 77 kDa
MWexpected 79 kDa
VPorod 117 nm3
log I(s) 1.92×103 1.92×102 1.92×101 1.92×100
transglutaminase 2 small angle scattering data  s, nm-1
ln I(s)
transglutaminase 2 Guinier plot ln 1.92×103 Rg: 3.4 nm 0 (3.4 nm)-2 s2
(sRg)2I(s)/I(0)
transglutaminase 2 Kratky plot 1.104 0 √3 sRg
p(r)
transglutaminase 2 pair distance distribution function Rg: 3.4 nm 0 Dmax: 12 nm

Data validation

Fits and models

log I(s)
 s, nm-1
transglutaminase 2 CRYSOL model
log I(s)
 s, nm-1
Synchrotron SAXS data from solutions of transglutaminase-2 (TGA2) in 20 mM Tris 150mM NaCl 1mM EDTA, pH 7.2 were collected on the EMBL P12 beam line at the PETRA III storage ring (DESY; Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3.1 m and at a wavelength of λ = 0.12 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.50 mg/ml was measured at 10°C. 20 successive 0.050 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.

Structural basis for antigen recognition by transglutaminase 2-specific autoantibodies in celiac disease --- this is the scattering profile of TG2 by itself that is comprised primarilly of monomers and higher oligomeric species (monomer 92%; dimer 8% volume fraction.)

transglutaminase 2 (TGA)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   79.5 kDa
Sequence   FASTA