Druggability of methyl-lysine binding sites |
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Authors: | C. Santiago K. Nguyen M. Schapira |
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Affiliation: | (1) Structural Genomics Consortium, University of Toronto, Toronto, ON, Canada;(2) Structural Genomics Consortium, and Department of Pharmacology, University of Toronto, Toronto, ON, Canada; |
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Abstract: | Structural modules that specifically recognize—or read—methylated or acetylated lysine residues on histone peptides are important components of chromatin-mediated signaling and epigenetic regulation of gene expression. Deregulation of epigenetic mechanisms is associated with disease conditions, and antagonists of acetyl-lysine binding bromodomains are efficacious in animal models of cancer and inflammation, but little is known regarding the druggability of methyl-lysine binding modules. We conducted a systematic structural analysis of readers of methyl marks and derived a predictive druggability landscape of methyl-lysine binding modules. We show that these target classes are generally less druggable than bromodomains, but that some proteins stand as notable exceptions. |
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