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