Comment on "Structural basis of histone H3K27 trimethylation by an active polycomb repressive complex 2"

被引：18

作者：

Zhang, Ying ^{[1
]}

Justin, Neil ^{[1
]}

Wilson, Jon R. ^{[1
]}

Gamblin, Steven J. ^{[1
]}

机构：

[1] Francis Crick Inst, 1 Midland Rd, London NW1 1AT, England

来源：

SCIENCE | 2016年 / 354卷 / 6319期

基金：

英国惠康基金;

关键词：

LYSINE METHYLTRANSFERASE; INHIBITION; CANCER; PRC2; MUTATION;

D O I：

10.1126/science.aaf6236

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Jiao and Liu (Research Articles, 16 October 2015, aac4383) reported the crystal structure of the protein complex polycomb repressive complex 2 from Chaetomium thermophilum. This landmark structure has brought invaluable insights into the activation mechanism of this essential methyltransferase. However, the analysis of the x-ray data discussed below suggests that the description of oncogenic H3K27M peptide binding to the active site is incorrect. © 2016 by the American Association for the Advancement of Science; all rights reserved.

引用

页数：3

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