Structural basis for site-specific reading of unmodified R2 of histone H3 tail by UHRF1 PHD finger
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.
PHD、reading、structures、complex、two、NMR
21
R329.2(人体形态学)
National Basic Research Program of China2009CB918600;2011CB966300;National Natural Science Foundation of China20921091;Pujiang Talents Awards from Science and Technology Commission of Shanghai Municipality08PJ1411700
2011-12-05(万方平台首次上网日期,不代表论文的发表时间)
1379-1382