2. Academic Validation
  3. Nucleoside protein arginine methyltransferase 5 (PRMT5) inhibitors

Nucleoside protein arginine methyltransferase 5 (PRMT5) inhibitors

  • Bioorg Med Chem Lett. 2019 Jun 1;29(11):1264-1269. doi: 10.1016/j.bmcl.2019.03.042.
Hong Lin 1,  Juan I Luengo 1
Affiliations

Affiliation

  • 1 Prelude Therapeutics, 200 Powder Mill Road, Wilmington, DE 19803, United States.
PMID: 30956011 DOI: 10.1016/j.bmcl.2019.03.042
Abstract

Protein Arginine Methyltransferase 5 (PRMT5) is known to symmetrically dimethylate numerous cytosolic and nuclear proteins that are involved in a variety of cellular processes. Recent findings have revealed its potential as a Cancer therapeutic target. PRMT5 selective inhibitors, GSK3326595, a substrate competitive inhibitor, and JNJ64619178, a SAM (S-adenosyl-l-methionine) mimetic/competitive inhibitor, have entered clinic trials for multiple Cancer types. This review focuses on the recent developments in SAM mimetic nucleoside PRMT5 inhibitors, their SAR and structural insight based on published co-crystal structures.

Keywords

Nucleoside; PRMT5; SAR.

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