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. 2017 Jul 17;114(31):8229–8234. doi: 10.1073/pnas.1702192114

Fig. 2.

Fig. 2.

The catalytic domain of TET3 and the AF2 domain of TRα1 confer the interaction between these two proteins. (A) Schematic representation and summary of interactions of full-length and truncation mutants of TET3 and TRα1. AF2, activation function domain 2; Cat, catalytic domain; CRD, cysteine-rich domain; CXXC, CXXC domain; DSBH, double-stranded beta-helix domain; DBD, DNA binding domain; LBD, ligand binding domain. “+,” more “+,” and “−” represent, respectively, interaction, stronger interaction, and no interaction. (B and C) Characterization of the interacting regions in TET3 with TRα1. Whole-cell extracts were prepared from HEK293T cells expressing indicated proteins. (B) GS-TRα1 was precipitated with M280 beads; coprecipitated F-TET3 mutants were detected using anti-Flag antibody. Asterisk indicates bands for TRα1 that are recognized thanks to the cross-reaction between anti-Flag antibody and its GS tag. (C) Flag beads were used to precipitate TET3 truncation mutants; coprecipitated TRα1 was detected with anti-GFP antibody. (D) Characterization of the interacting regions in TRα1 with TET3. Flag beads were used to precipitate TRα1 truncation mutants; coprecipitated TET3 was detected with anti-Myc antibody.