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. 2020 Sep 3;11:579636. doi: 10.3389/fgene.2020.579636

FIGURE 2.

FIGURE 2

Implications of asparaginyl hydroxylation within the ARDs of G9a and GLP methyltransferases. (A) Crystal structure of G9a-like protein (GLP) ankyrin repeat domain (ARD) domain in complex with dimethylated H3 N-terminal tail visualized with PyMOL (PDB ID, 3B95; Collins et al., 2008). Binding of a dimethylated peptide (orange backbone) is mediated by the hydrophobic binding cage (blue) and H3-S10/T11 interacting residues (IRs; green) of the GLP ARD (white, cartoon representation). The GLP(N867) hydroxylation site (pink) is distant from the peptide binding region and is adjacent to the D865 residue (red). (B) The proximity of the D865 and N867 residues, where the target hydroxylated atom (i.e., β-carbon of N867) is denoted by an asterisk. (C) Sequence similarity between G9a and GLP asparaginyl hydroxylated regions, up- and downstream ten residues from the modified asparagine (bold, underlined). Candidate hydrogen bonding aspartates (red) occur two residues upstream the G9a-N779 and GLP-N867 hydroxylation sites.