Journal of Molecular Endocrinology

Coregulator complexes are recruited to the genome through DNA-binding transcription factors such as nuclear receptors. (A) Cartoon to illustrate the recruitment of coactivator complex to genes by liganded nuclear receptors, resulting in the acetylation of histone tails and an increase in the rate of transcription. (B) Nuclear receptors recruit corepressor complexes in the absence of ligand, resulting in the deacetylation of histone tails and decrease in the rate of transcription. (C) Crystal structure of PPARγ (light blue) and RXRα (yellow) heterodimer bound to DNA with an NCOA2 peptide (green). Ligands rosiglitazone (for PPARγ and 9-cis retinoic acid (for RXRα are shown as purple sticks). Zinc atoms are shown as grey spheres (PDB code 3DZY (Chandra et al. 2008)). (D) Structure of PPARγ LBD (light blue) with the ligand rosiglitazone (pink) bound to a peptide from the SRC1 coactivator (green) (PDB code 2PRG (Nolte et al. 1998)). (E) Structure of PPARα LBD (light blue) with the antagonist GW6471 (pink) bound to a peptide from the SMRT corepressor (red) (PDB code 1KKQ (Xu et al. 2002)). Helix 12 is highlighted in yellow in both (D and E).