A combinatorial approach to characterize the substrate specificity of protein arginine methyltransferase 1
Department of Biochemistry and Molecular Pharmacology
Medical Subject Headings
Amino Acid Sequence; Enzyme Inhibitors; Humans; Molecular Sequence Data; Peptide Library; Protein-Arginine N-Methyltransferases; Substrate Specificity
Biochemistry | Enzymes and Coenzymes | Medicinal-Pharmaceutical Chemistry | Therapeutics
The dysregulation of protein arginine methyltransferases (PRMTs) is implicated in a wide variety of disease states. Here we report the design, synthesis, and screening of a combinatorial peptide library used to characterize the substrate specificity of PRMT1. The information gained from this approach was used to develop a PRMT1 inhibitor with enhanced selectivity.
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Citation: Mol Biosyst. 2011 Jan;7(1):48-51. doi: 10.1039/c0mb00015a. Link to article on publisher's site. Epub 2010 Jul 6.
Bicker, Kevin L.; Obianyo, Obiamaka; Rust, Heather L.; and Thompson, Paul R., "A combinatorial approach to characterize the substrate specificity of protein arginine methyltransferase 1" (2011). Thompson Lab Publications. 55.