Description
Protein arginine N-methyltransferase 3 (PRMT3, ) is a predominantly cytoplasmic enzyme that is constitutively expressed. SGC707 is a potent, selective allosteric inhibitor of PRMT3 (IC
50 = 50 nM). It inhibits the methylation of histones in cells with an IC
50 value below 1 μM. XY1 is a close analog of SGC707 that is completely inactive against PRMT3 at concentrations as high as 100 μM. It is intended to be used as a negative control for SGC707 in studies involving PRMT3 action. See the
Structural Genomics Consortium (SGC) website for more information.
References
[1] J TANG. PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation.[J]. The Journal of Biological Chemistry, 1998, 273 27: 16935-16945. DOI:
10.1074/jbc.273.27.16935[2] WOLF S S. The protein arginine methyltransferase family: an update about function, new perspectives and the physiological role in humans.[J]. Cellular and Molecular Life Sciences, 2009, 66 13: 2109-2121. DOI:
10.1007/s00018-009-0010-x[3] DR. H. üMIT KANISKAN. A Potent, Selective and Cell-Active Allosteric Inhibitor of Protein Arginine Methyltransferase 3 (PRMT3)[J]. Angewandte Chemie International Edition, 2015, 54 17: 5166-5170. DOI:
10.1002/anie.201412154
