Fig. 8: TGM6 residues responsible for its high affinity for TGFBR2. | Nature Communications

Fig. 8: TGM6 residues responsible for its high affinity for TGFBR2.

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

Fig. 8: TGM6 residues responsible for its high affinity for TGFBR2.The alternative text for this image may have been generated using AI.

ITC fitted binding isotherms (top) and residuals (bottom) for titration of TGM6-D3 KSGT (a) or TGM1-D3 QRRG (b) into TGFBR2. Fitted binding isotherms are overlaid as two experiments shaded purple and blue. Inhibition of TGF-β1 signaling in MFB-F11 fibroblasts as detected by the conversion of p-nitrophenylphosphate by secreted alkaline phosphatase (c, d) or by pSMAD2 western blotting (e) by either TGM6 (c, e) or TGM6 KSGT (d, e). In the MFB-F11 assay, the cells were stimulated with 0, 40, or 200 pM TGF-β1 (blue, yellow, and orange symbols, respectively). Activation of TGF-β1 signaling in MFB-F11 fibroblasts as detected by the conversion of p-nitrophenylphosphate by secreted alkaline phosphatase (f, g) or by pSMAD2 western blotting (h, i) by either TGM1 or TGM1 QRRG (f, h) or by TGM1-D123 or TGM1-D123 QRRG (g, i). Data shown in (c, d, f, g) are mean and standard deviation of triplicate measurements from one experiment. Blots shown in (e, h, i) are from one experiment with α-tubulin serving as a loading control. Source data of (a, b) and (c, i) provided through Figshare [https://doi.org/10.6084/m9.figshare.28179359] or the Source Data file associated with the article, respectively.

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