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

SASDGG2 – Interleukin 11 receptor subunit alpha

Interleukin-11 receptor subunit alpha
MWexperimental 34 kDa
MWexpected 32 kDa
VPorod 41 nm3
log I(s) 1.05×10-2 1.05×10-3 1.05×10-4 1.05×10-5
Interleukin-11 receptor subunit alpha small angle scattering data  s, nm-1
ln I(s)
Interleukin-11 receptor subunit alpha Guinier plot ln 1.06×10-2 Rg: 3.0 nm 0 (3.0 nm)-2 s2
Interleukin-11 receptor subunit alpha Kratky plot 1.104 0 3 sRg
Interleukin-11 receptor subunit alpha pair distance distribution function Rg: 3.1 nm 0 Dmax: 9.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Interleukin-11 receptor subunit alpha PDB model

Synchrotron SAXS data from solutions of the alpha subunit of the interleukin 11 receptor 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 2.5 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 sample at 2.7 mg/ml was injected at a 0.45 ml/min flow rate onto a GE Superdex 200 Increase 5/150 column at 20°C. Six 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.

Interleukin-11 receptor subunit alpha (IL11RA)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   32.2 kDa
UniProt   Q14626 (23-319)
Sequence   FASTA
PDB code   6O4P