Adaptability and selectivity of human peroxisome proliferator-activated receptor (PPAR) pan agonists revealed from crystal structures

Oyama, T.; Toyota, K.; Waku, T.; Hirakawa, Y.; Nagasawa, N.; Kasuga, J.; Hashimoto, Y.; Miyachi, H.; Morikawa, K.

doi:10.1107/S0907444909015935

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 3
Comparison between the PPARα LBD–TIPP-703 and the PPARγ LBD–TIPP-703 complexes. (a) Stereoview of the superimposed structures. The PPARα LBD–TIPP-703 complex is coloured cyan and the PPARγ LBD–TIPP-703 complex is coloured green. The key contact residues in the complexes are highlighted. Prominent interactions in each complex are indicated by arrows. (b) Schematic view of the protein–ligand interactions. A structure-based sequence alignment was generated around the ligand-binding pocket. In the PPARα and PPARγ sequences, the residues that interact with TIPP-703 are coloured blue (hydrophobic) and red (hydrophilic).

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 65| Part 8| July 2009| Pages 786-795

doi:10.1107/S0907444909015935

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