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

• 来源期刊: 细胞研究（英文版）
• 年，卷（期）: 2011,（9）
• 页码范围: 1379-1382
• 页数: 4页
• 语种: 英文
• DOI: 10.1038/cr.2011.123

摘要

Dear Editor,We report two NMR complex structures of PHDUHRF1 binding to unmodified or K9 trimethylated histone tails,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.