Structural basis for site-specific reading of unmodified R2 of histone H3 tail by UHRF1 PHD finger  

作　　者：ChengkunWang  JieShen  ZhongzhengYang  PingChen  BinZhao  WeiHu  WenxianLan  XiaotianTong  HoumingWu  GuohongLi ChunyangCao 

机构地区：[1]State Key Laboratory of Bio-organic and Natural Product Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 200032, China [2]National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China

出　　处：《Cell Research》2011年第9期1379-1382,共4页细胞研究(英文版)

摘　　要：Dear Editor, We report two NMR complex structures of PHDUHRF1 binding to unmodified or K9 trimethylated histone mils, which clarify a controversy regarding how the binding of UHRF1 to H3 tails is mediated. Based on our structures, H3R2, not H3K9, mediates PHD binding.

关 键 词：组蛋白H3 PHD 结构 修改 基础 阅读 尾部 站点 

分 类 号：S511[农业科学—作物学] TP273[自动化与计算机技术—检测技术与自动化装置]