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. Author manuscript; available in PMC: 2011 Dec 1.
Published in final edited form as: Expert Rev Proteomics. 2011 Feb;8(1):43–59. doi: 10.1586/epr.10.109

Figure 3. Differential hydrogen/deuterium exchange coupled with mass spectrometry data for peroxisome proliferator-activated receptor γ-ligand binding domain ± rosiglitazone and MRL24.

Figure 3

The HDX data shown correspond to four regions of interest: helix 3 (IRIFQGCQF), the β-sheet region (ISEGQGFMTRE), helix 12 (QEIYKDLY) and the helix 2–2′ link region containing the site of CDK5 phosphorylation (KTTDKSPFVIYDM). (A) Histograms showing the percent reduction in HDX for each peptide region. Values are calculated relative to the measured %D value for apo peroxisome proliferator-activated receptor (PPAR)γ-LBD (n = 4; error bars are standard error of the mean; p < 0.01, p < 0.001). (B) HDX data for the four peptides of interest are plotted over the structures of PPARγ-LBD bound with rosiglitazone (left: PDB:2PRG) and MRL24 (right: PDB:2Q5P). Percent reduction in HDX relative to apo receptor is colored according to the key. Red circle indicates Ser273 residue of PPARγ.

H12: Helix 12; HDX: Hydrogen/deuterium exchange; LBD: Ligand-binding domain; ns: Not significant.

Reproduced with permission from [79].