Solution Structures of PPARγ2/RXRα Complexes

Figure 1

Biophysical characterization of the stoichiometry of the TIF2 RID/PPARγ/RXR complexes. (a) Structural organization of hPPARγ1, hPPARγ2, and hTIF2. (b) ESI mass spectra of TIF2 RID/PPARγ/RXR LBDs recorded under nondenaturing conditions in 200 mM ammonium acetate at pH=7.4. The different charge states of the proteins are indicated above the peaks. The calculated molecular mass of the first peak corresponds to PPARγ/RXRα LBDs and the second one to the complex containing one PPARγ/RXRα LBDs dimer and one TIF2 RID. (c) Sedimentation equilibrium experiments. Best fits of experimental data for TIF2 RID/PPARγΔNTD/RXRΔNTD at 12,000 rpm with the self-association methods (SedPhat program). Sedimentation equilibrium data agrees with one TIF2 RID bound to PPARγΔNTD/RXRΔNTD.

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