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. 2017 Jul 19;158(9):3067–3078. doi: 10.1210/en.2017-00314

Figure 4.

Figure 4.

LBD domain exchange between THRA1 and THRB2 affects receptor binding to DR4 and LAP. (a and c) Schematic structures and (b and d) protein levels of in vitro–translated THRA1, THRA1LBD, THRB2, and THRB2LBD are shown. pSP72 was used as an “empty” vector negative control. (e–h) EMSA of chimeric receptors in the absence and presence of RXRA. (e) On DR4, neither THRA1 nor THRA1LBD formed a homodimer. (g) THRA1LBD formed a stronger homodimer than did WT THRA1 and did not dissociate from LAP after T3 treatment. Both THRA1 and THRA1LBD formed heterodimers with RXRA on DR4 and LAP. (f) On DR4, the THRBLBD lost the ability to form a homodimer compared with that of WT THRB2. (h) In contrast to WT THRB2, THRB2LBD partially dissociated from the LAP element after T3 treatment. THRB2 and THRB2LBD showed similar abilities to form heterodimers with RXRA on both DNA elements. Samples were treated with vehicle or increasing concentrations of T3 (1 nM, 10 nM, and 100 nM). *Nonspecific band observed in unprogrammed lysate.