Structure of the arginine methyltransferase PRMT5-MEP50 reveals a mechanism for substrate specificity.

Structure of the arginine methyltransferase PRMT5-MEP50 reveals a mechanism for substrate specificity.

The arginine methyltransferase PRMT5-MEP50 is required for embryogenesis and is misregulated in many cancers. PRMT5 targets a wide variety of substrates, including histone proteins involved in specifying an epigenetic code. However, the mechanism by which PRMT5 utilizes MEP50 to discriminate substra...

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Bibliographic Details
Main Authors:	Meng-Chiao Ho, Carola Wilczek, Jeffrey B Bonanno, Li Xing, Janina Seznec, Tsutomu Matsui, Lester G Carter, Takashi Onikubo, P Rajesh Kumar, Man K Chan, Michael Brenowitz, R Holland Cheng, Ulf Reimer, Steven C Almo, David Shechter
Format:	Article
Language:	English
Published:	Public Library of Science (PLoS) 2013-01-01
Series:	PLoS ONE
Online Access:	http://europepmc.org/articles/PMC3581573?pdf=render

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