Structural context of disease-associated mutations and putative mechanism of autoinhibition revealed by X-ray crystallographic analysis of the EZH2-SET domain.

Structural context of disease-associated mutations and putative mechanism of autoinhibition revealed by X-ray crystallographic analysis of the EZH2-SET domain.

The enhancer-of-zeste homolog 2 (EZH2) gene product is an 87 kDa polycomb group (PcG) protein containing a C-terminal methyltransferase SET domain. EZH2, along with binding partners, i.e., EED and SUZ12, upon which it is dependent for activity forms the core of the polycomb repressive complex 2 (PRC...

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Bibliographic Details
Main Authors: Stephen Antonysamy, Bradley Condon, Zhanna Druzina, Jeffrey B Bonanno, Tarun Gheyi, Feiyu Zhang, Iain MacEwan, Aiping Zhang, Sheela Ashok, Logan Rodgers, Marijane Russell, John Gately Luz
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2013-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3868555?pdf=render

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http://europepmc.org/articles/PMC3868555?pdf=render

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