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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Главные авторы: Ho, Meng-Chiao, Wilczek, Carola, Bonanno, Jeffrey B., Xing, Li, Seznec, Janina, Matsui, Tsutomu, Carter, Lester G., Onikubo, Takashi, Kumar, P. Rajesh, Chan, Man K., Brenowitz, Michael, Cheng, R. Holland, Reimer, Ulf, Almo, Steven C., Shechter, David
Формат: Artigo
Язык:Inglês
Опубликовано: Public Library of Science 2013
Предметы:
Research Article
Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC3581573/
https://ncbi.nlm.nih.gov/pubmed/23451136
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1371/journal.pone.0057008
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