%0 Figure %A Walker, Ryan %A Czepnik, Magdalena %A Goebel, Erich %A McCoy, Jason %A Vujic, Ana %A Cho, Miook %A Oh, Juhyun %A Aykul, Senem %A Walton, Kelly %A Schang, Gauthier %A Bernard, Daniel %A Hinck, Andrew %A Harrison, Craig %A Martinez-Hackert, Erik %A Wagers, Amy %A Lee, Richard %A Thompson, Thomas %D 2017 %T Additional file 5: Figure S4. of Structural basis for potency differences between GDF8 and GDF11 %U https://springernature.figshare.com/articles/figure/Additional_file_5_Figure_S4_of_Structural_basis_for_potency_differences_between_GDF8_and_GDF11/4724605 %R 10.6084/m9.figshare.c.3709096_D5.v1 %2 https://springernature.figshare.com/ndownloader/files/7712701 %K Ligands %K Myostatin %K Receptor %K Structure %K Transforming growth factor β (TGFβ) %X Binding of GDF11 to the type I receptor ALK5. A, B, C Steady state analysis for SPR traces shown in Fig. 7b and calculated values. The maximum response at each concentration is plotted to a steady state binding equation using Biacore T200 Evaluation Software version 1.0 (Biacore). Sensorgrams were double referenced using an average of two 0 nM ligand injections. Ligand sources: GDF8 and GDF11, gift from Acceleron Pharma; Activin A, Activin B, and TGFβ3, produced and purified as described in “Methods.” D, E, F Ligand binding to Fc-ActRIIB-ECD (A), Fc-ALK5-ECD (B), and ALK5-ECD (C) amine coupled to a CM5 biosensor chip. Ligands were at 500 nM. TβRII, the type II receptor, was required for TGFβ3 binding to Fc-ALK5-ECD and ALK5-ECD. The receptor concentration was at 1 μM for this experiment. Experiments were performed using 40 μL/min flow rate at 37 °C. (TIF 1166 kb) %I figshare