Structure-Based VS for Histone Arginine Methyltransferase PRMT1 Inhibitors

Structure-Based VS for Histone Arginine Methyltransferase PRMT1 Inhibitors 

Histones are subject to a whole set of different posttranslational modifications that set a pattern of molecular signals for the access of transcription factors toward DNA, the so-called histone code [28]. The histone N-termini, which are rich in arginine and lysine residues, protrude out of the histone octamers and undergo various types of posttranslational modifications such as acetylation, methylation, phosphorylation. 

We observed the same binding mode in the crystal structures and in the homology model for both the cofactor and the arginine side chain. 

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