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. Author manuscript; available in PMC: 2012 Jan 1.
Published in final edited form as: Nat Struct Mol Biol. 2011 Jun 12;18(7):769–776. doi: 10.1038/nsmb.2062

Figure 3. Molecular basis for H3K9me3 recognition by ADDATRX.

Figure 3

(a) Ribbon representation of ADDATRX domain in complex with H31–15K9me3 peptide. ADDATRX domain is a hybrid of a GATA-like zinc finger (cyan) and a PHD finger (magenta). Three zinc ions are depicted as spheres and the H3 peptide is colored yellow with key residues Lys4 and K9me3 shown in stick representation. (b) Surface electrostatic view of ADDATRX domain in complex with H31–15K9me3 peptide, color-coded with red representing negatively-charged and blue positively-charged potentials. The Fo-Fc omit map was contoured at 3.5 σ level for the bound H3 peptide. (c) Stereo view of the K9me3-binding pocket. The GATA-like segment Tyr203–Ser210 and the PHD finger segment Gln219–-Glu225 are color-coded in cyan and magenta, respectively. Blue dotted lines refer to nonconventional C-H:O hydrogen bonds. (d) A snug fit of the bulky trimethyllysine group inserted into the reader pocket of ADDATRX.