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

SASDLR3 – Interleukin 11 Mutein

Interleukin 11 Mutein
MWexperimental 17 kDa
MWexpected 18 kDa
VPorod 25 nm3
log I(s) 6.62×10-3 6.62×10-4 6.62×10-5 6.62×10-6
Interleukin 11 Mutein small angle scattering data  s, nm-1
ln I(s)
Interleukin 11 Mutein Guinier plot ln 6.62×10-3 Rg: 1.8 nm 0 (1.8 nm)-2 s2
(sRg)2I(s)/I(0)
Interleukin 11 Mutein Kratky plot 1.104 0 √3 sRg
p(r)
Interleukin 11 Mutein pair distance distribution function Rg: 1.8 nm 0 Dmax: 5.4 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Interleukin 11 Mutein OTHER model
Synchrotron SAXS data from solutions of Interleukin 11 Mutein 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 3.5 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 0.45 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 22°C. Nine 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 Mutein
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   18.3 kDa
Sequence   FASTA
 
PDB ID   8DPW