Structural basis for IL-33 recognition and its antagonism by the helminth effector protein HpARI2.

Jamwal A, Colomb F, McSorley HJ, Higgins MK, Nat Commun 15(1):5226 (2024) Europe PMC

SASDUW6 – Alarmin release inhibitor (HpARI2), full-length

Alarmin release inhibitor (Δ1-62)
MWI(0) 22 kDa
MWexpected 26 kDa
VPorod 31 nm3
log I(s) 4.25×10-2 4.25×10-3 4.25×10-4 4.25×10-5
Alarmin release inhibitor (Δ1-62) small angle scattering data  s, nm-1
ln I(s)
Alarmin release inhibitor (Δ1-62) Guinier plot ln 4.25×10-2 Rg: 2.6 nm 0 (2.6 nm)-2 s2
(sRg)2I(s)/I(0)
Alarmin release inhibitor (Δ1-62) Kratky plot 1.104 0 3 sRg
p(r)
Alarmin release inhibitor (Δ1-62) pair distance distribution function Rg: 2.8 nm 0 Dmax: 9.9 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Alarmin release inhibitor (Δ1-62) DAMMIF model

log I(s)
 s, nm-1
Alarmin release inhibitor (Δ1-62) CHIMERA model

Synchrotron SAXS data from solutions of alarmin release inhibitor in 137 mM NaCl, 2.7 mM KCl, 10 mM phosphate buffer, 5% glycerol, pH 7.2 were collected on the B21 beam line at the Diamond Light Source (Didcot, UK) using a Eiger 4M detector at a sample-detector distance of 3.7 m and at a wavelength of λ = 0.09464 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 8.00 mg/ml was measured at 15°C. 600 successive 3 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.

Alarmin release inhibitor (Δ1-62) (HpARI2)
Mol. type   Protein
Organism   Heligmosomoides polygyrus
Olig. state   Monomer
Mon. MW   26.0 kDa
 
UniProt   A0A3P7XL18 (63-297)
Sequence   FASTA