Fig. 3: TGM6-D3, and TGM1-D3, compete with TGF-β for binding TGFBR2. | Nature Communications

Fig. 3: TGM6-D3, and TGM1-D3, compete with TGF-β for binding TGFBR2.

From: TGM6 is a helminth secretory product that mimics TGF-β binding to TGFBR2 to antagonize signaling in fibroblasts

Fig. 3: TGM6-D3, and TGM1-D3, compete with TGF-β for binding TGFBR2.The alternative text for this image may have been generated using AI.

a Titration of TGFBR2 into mmTGF-β2-7M2R in the absence (purple) or presence (blue) of 6 μM TGM6-D3 as the lower-affinity binder. b Titration of TGFBR2 into TGM6-D3 in the absence (purple) or presence (blue) of 6 μM TGM1-D3 as the lower-affinity binder. Thermograms in (a, b) are presented as single experiment without (purple) and with (blue) competitor. Each panel includes the thermograms (top), mean integrated heats ± SD and fitted isotherms (middle), and fitting residuals (bottom) for the associated titrations. The data were globally fit using a simple competitive binding model. Source data of (a, b) provided through Figshare [https://doi.org/10.6084/m9.figshare.28179359].

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