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. Author manuscript; available in PMC: 2014 Mar 24.
Published in final edited form as: J Mol Endocrinol. 2013 Nov 7;51(3):T23–T36. doi: 10.1530/JME-13-0227

Figure 2.

Figure 2

Crystal structures of coregulator proteins possessing enzymatic activity with schematic representations of their cognate complexes. (A) The histone deacetylase HDAC1 bound to an MTA1 dimer, with sulphate molecules bound at the positively charged inositol phosphate-binding interface between the two proteins (pdb code 4BKX (Millard et al. 2013)). (B) The histone acetyltransferase p300 with inhibitor Lys-CoA (pdb code 3BIY (Liu et al. 2008)). In all panels: enzymes are shown in green, accessory proteins in blue, metal ions in grey and histone tails/cofactors as pink spheres. (C) The arginine methytransferase PRMT5 in complex with the adaptor protein MEP50 with bound AdoMet analogue and H4 peptide (pdb code 4GQB (Antonysamy et al. 2012)). (D) The demethylase LSD1 with corepressor CoREST. A histone H3 peptide covalently attached to FAD is bound in the active site of LSD1 (pdb code 2UXN (Yang et al. 2007)). (E) The ATPase domain from CHD1 with a bound nucleotide (pdb code 3MWY (Hauk et al. 2010)).