Structures of the interleukin 11 signalling complex reveal gp130 dynamics and the inhibitory mechanism of a cytokine variant

Metcalfe R, Hanssen E, Fung K, Aizel K, Kosasih C, Zlatic C, Doughty L, Morton C, Leis A, Parker M, Gooley P, Putoczki T, Griffin M, Nature Communications 14(1) (2023) DOI

SASDLQ3 – Interleukin 11, W168A mutant

Interleukin-11 (W168A)
MWexperimental 17 kDa
MWexpected 18 kDa
VPorod 22 nm3
log I(s) 5.09×10-3 5.09×10-4 5.09×10-5 5.09×10-6
Interleukin-11 (W168A) small angle scattering data  s, nm-1
ln I(s)
Interleukin-11 (W168A) Guinier plot ln 5.10×10-3 Rg: 1.7 nm 0 (1.7 nm)-2 s2
(sRg)2I(s)/I(0)
Interleukin-11 (W168A) Kratky plot 1.104 0 √3 sRg
p(r)
Interleukin-11 (W168A) pair distance distribution function Rg: 1.7 nm 0 Dmax: 5.2 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Interleukin-11 (W168A) OTHER model
Synchrotron SAXS data from solutions of Interleukin 11, W168A mutant in 20 mM Tris, 150 mM NaCl, 0.2% sodium azide, pH 8.5 were collected on the SAXS/WAXS beam line at the Australian Synchrotron storage ring (Melbourne, Australia) using a Pilatus3 S 2M detector at a sample-detector distance of 2.2 m and at a wavelength of λ = 0.108 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 sample at 5 mg/ml was injected at a 0.40 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 22°C. 13 successive 1 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.

Sample injection volume = UNKNOWN

Interleukin-11 (W168A) (IL11(W168A))
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   18.1 kDa
 
UniProt   P20809 (32-199)
Sequence   FASTA
 
PDB ID   8DPV