Supplementary Figure 2: Structural comparisons of PHD and RING domains.
From: Structure of the p300 catalytic core and implications for chromatin targeting and HAT regulation
(a) Structure of the BPTF PHD domain bound to H3K4me3. (b) Superimposed structures of p300 PHD (red), Pygo (2VPE, green), BPTF (3qvz, orange), ING2 (2G6Q, blue). The PHD domain is most similar to the PHD domain of BPTF. (c) Structure–based sequence alignment of the PHD domain. Zinc ligand positions are shown as red boxes. Residues that make up the aromatic cage are shown as a blue box and labeled I–IV. Residues that make specific contacts with the H3K4me2/3 peptide are shown in green. (d) The RING domain is similar to other RING structures. Superimposed structures of p300 RING (green) and Cbl RING domain (red). The p300 RING domain is missing the second Zinc binding site. The sequence insertion in loop L1 is shown. (e) Structure–based sequence alignment of the RING domain. Zinc ligand positions as above. Residues that make specific contacts with E2 enzymes are shown in blue. 3MMK: Residues 56–290 are omitted from the alignment.
