The structure of the extracellular domains of human interleukin 11 α-receptor reveals mechanisms of cytokine engagement

Metcalfe R Aizel K, Zlatic C, Nguyen P, Morton C, Lio D, Cheng H, Dobson R, Parker M, Gooley P, Putoczki T, Griffin M, Journal of Biological Chemistry :jbc.RA119.012351 (2020) DOI

SASDGH2 – Interleukin 11, N-terminally truncated

Interleukin 11
MWexperimental 16 kDa
MWexpected 18 kDa
VPorod 22 nm3
log I(s) 6.12×10-3 6.12×10-4 6.12×10-5 6.12×10-6
Interleukin 11 small angle scattering data  s, nm-1
ln I(s)
Interleukin 11 Guinier plot ln 6.12×10-3 Rg: 1.7 nm 0 (1.7 nm)-2 s2
(sRg)2I(s)/I(0)
Interleukin 11 Kratky plot 1.104 0 √3 sRg
p(r)
Interleukin 11 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 PDB (PROTEIN DATA BANK) model
Synchrotron SAXS data from solutions of N-terminally truncated interleukin 11 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 (Melbourne, Australia) using a Dectris/Pilatus3 S 2M detector at a sample-detector distance of 2.0 m and at a wavelength of λ = 0.1078 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 50.00 μl sample at 5 mg/ml was injected at a 0.45 ml/min flow rate onto a GE Superdex 200 Increase 5/150 column at 20°C. Eight successive 1 second frames were collected through the SEC elution peak of the sample. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Storage temperature = UNKNOWN

Interleukin 11 (IL11)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   18.2 kDa
 
UniProt   A8K3F7 (32-199)
Sequence   FASTA
 
PDB ID   6O4O