The protein methyltransferases (PMTs) represent a large class of enzymes that catalyse the methylation of side chain nitrogen atoms of the amino acids lysine or arginine at specific locations along the primary sequence of target proteins. These enzymes play a key role in the spatio-temporal control of gene transcription by performing site-specific methylation of lysine or arginine residues within the histone proteins of chromatin, thus effecting chromatin conformational changes that activate or repress gene transcription. The dysregulated activity of some PMTs plays an oncogenic role in a number of human cancers. The past decade has seen significant progress made in the discovery and optimization of small-molecule inhibitors of a number of cancer-associated PMTs such as protein arginine methyltransferases (PRMTs). Examples of such compounds bind in the SAM binding pocket of PMTs and behave as SAM competitive inhibitors. 
Reference database includes more than 100 small molecule compounds with reported affinity against PRMTs. The focused library has been collected based on privileged substructure searching including core-head containing analogues, 2D-topological pharmacophore modeling, isosteric morphing and structure similarity searching (Tanimoto) as well as diversity sub-set.
 R. A. Copeland, “Protein methyltransferase inhibitors as precision cancer therapeutics: A decade of discovery,” Philos. Trans. R. Soc. B Biol. Sci., vol. 373, no. 1748, 2018, doi: 10.1098/rstb.2017.0080.
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