Fig. 12

Structure of N-CoR ID1 peptide and interactions. a N-CoR ID1CoRNR peptide (pink) bound to Rev-erb αΔ 323-423 LBD (sea green; PDB 3N00) depicting the N-CoR ID1 peptide β-strand (β1N) and α-helix (α1N) and the new C-terminal β-strand sY of Rev-erb α LBD. The backbone of the contact residues in H3, H4, H5, and the new Yβ-strand are shown in yellow and the supporting H3 residues in orange. b Representation of the amino acid residue positions in the N-CoR ID1 peptide defining the new extended motif for NRCoR. c Comparison of the N-CoR ID1 CoRNR peptide (pink) bound to Rev-erb αΔ 323-423 LBD (sea green) with apo-Rev-erb β (gray) and heme (red)-bound Rev-erb β (yellow). The region within the black box represents the changes in H3 as a result of conformational changes in H11 when Rev-erb binds to N-CoR ID1/heme.