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. Author manuscript; available in PMC: 2016 Oct 26.
Published in final edited form as: Angew Chem Int Ed Engl. 2015 Sep 7;54(44):13085–13089. doi: 10.1002/anie.201506889

Figure 4.

Figure 4

(a) Structure of the pSTAT3 dimer: SH2 domain at the top, bound to a phosphopeptide ligand (wireframe) of the complementary molecule. The central DNA-binding domain bound to dsDNA (orange). The CCD is shown in the inset, with the site of rhodium-catalyzed labeling (Phe174) in purple and the Asp170 residue (green), identified previously as a residue controlling STAT3 function. See text for discussion. (b) STAT3 coiled-coil region, indicating a lack of Lewis-basic (H, M, C) residues (orange).