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. Author manuscript; available in PMC: 2021 Sep 28.
Published in final edited form as: Trends Biochem Sci. 2020 May 6;45(9):731–747. doi: 10.1016/j.tibs.2020.04.002

Figure 3: Lysine acylations are chemically diverse and recognized by unique domains.

Figure 3:

(A) Chemical structures for all identified histone lysine acylations. (B) Crystal structure diagram of Kcrotonyl in the YEATs domain binding pocket of H. sapiens AF9 (PDB: 5HJB). π-stacking is facilitated by residues F59 and Y78. (C) Crystal structure diagram of Kcrotonyl in the DPF domain binding pocket of H. sapiens MORF (PDB: 6OIE). S217 and S242 make polar contacts (mediated by a water molecule) with the crotonylated lysine. F218 improves specificity for Kcro over Kacetyl through π-stacking. (D) Crystal structure diagram of Kacetyl in the bromodomain binding pocket of H. sapiens BRPF1 (PDB: 5FFV). N708, a conserved residue in bromodomains, makes the sole polar contact with the acetylated lysine.