Fig. 5: Biophysical basis for IL-11 Mutein signalling inhibition. | Nature Communications

Fig. 5: Biophysical basis for IL-11 Mutein signalling inhibition.

From: Structures of the interleukin 11 signalling complex reveal gp130 dynamics and the inhibitory mechanism of a cytokine variant

Fig. 5: Biophysical basis for IL-11 Mutein signalling inhibition.The alternative text for this image may have been generated using AI.

A Continuous sedimentation coefficient (c(s)) distributions for the complexes formed between IL-11RαD1-D3, gp130D1-D3 and (i) IL-11Δ10/Mutein, (ii) IL-11Δ10/W147A, (iii) IL-11Δ10/PAIDY. Inlays show expanded detail of the 5–10 S region. B SAXS data for the IL-11RαD1-D3/gp130D1-D3/ IL-11Δ10 Mutein complex. The fit shown is to a model of the trimeric complex, χ2 1.7 (see Methods). C Representative ITC data for the interaction between IL-11RαD1-D3 and (i) IL-11Δ10/W147A, (ii) IL-11Δ10/Mutein, and (iii) IL-11Δ10/PAIDY. Representative of n = 3 independent experiments. D SPR data for the interaction between IL-11RαD1-D3 and (i) biotinylated IL-11Δ10/Mutein and (ii) biotinylated IL-11Δ10. Black lines show the fit to the data. Representative of n = 2 independent experiments. In both experiments, the biotin tag was used to immobilise IL-11Δ10 or IL-11Δ10 Mutein to a streptavidin sensor chip. For complete thermodynamic and kinetic parameters for the ITC and SPR experiments, see Supplementary Tables 4 and 5, respectively.

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