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