Journal
JOURNAL OF COMPUTER-AIDED MOLECULAR DESIGN
Volume 25, Issue 12, Pages 1171-1178Publisher
SPRINGER
DOI: 10.1007/s10822-011-9505-2
Keywords
Druggability; Binding pocket; Methyl-lysine; Inhibitors; Epigenetics
Categories
Funding
- Canadian Institutes for Health Research
- Canadian Foundation for Innovation
- Genome Canada through the Ontario Genomics Institute
- GlaxoSmithKline
- Eli Lilly
- Pfizer
- Novartis Research Foundation
- Life Technologies
- Ontario Innovation Trust
- Ontario Ministry for Research and Innovation
- Wellcome Trust
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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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