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J Comput Aided Mol Des. 2011 Dec;25(12):1171-8. doi: 10.1007/s10822-011-9505-2. Epub 2011 Dec 7.

Druggability of methyl-lysine binding sites.

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  • 1Structural Genomics Consortium, University of Toronto, Toronto, ON, Canada.


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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