An allosteric inhibitor of protein arginine methyltransferase 3.

  title={An allosteric inhibitor of protein arginine methyltransferase 3.},
  author={Alena Siarheyeva and Guillermo A. Senisterra and Abdellah Allali-Hassani and Aiping Dong and Elena Dobrovetsky and Gregory A. Wasney and Irene Chau and Richard Marcellus and Taraneh Hajian and Feng Liu and Ilia Korboukh and David Smil and Yuri Bolshan and Jinrong Min and Hong Qi Wu and Hong Zeng and Peter Loppnau and Gennadiy Poda and Carly Griffin and Ahmed M Aman and Peter J. C. Brown and Jian Jin and Rima Al-awar and Cheryl H. Arrowsmith and Matthieu Schapira and Masoud Vedadi},
  volume={20 8},
PRMT3, a protein arginine methyltransferase, has been shown to influence ribosomal biosynthesis by catalyzing the dimethylation of the 40S ribosomal protein S2. Although PRMT3 has been reported to be a cytosolic protein, it has been shown to methylate histone H4 peptide (H4 1-24) in vitro. Here, we report the identification of a PRMT3 inhibitor (1-(benzo[d][1,2,3]thiadiazol-6-yl)-3-(2-cyclohexenylethyl)urea; compound 1) with IC50 value of 2.5 μM by screening a library of 16,000 compounds using… CONTINUE READING
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