Structure insights into the molecular mechanism of the interaction between UHRF2 and PCNA
作者: Wanbiao ChenMinhao WuTianrong HangChengliang WangXuan ZhangJianye Zang
作者单位: 1Hefei National Laboratory for Physical Sciences at Microscale CAS Center for Excellence in Biomacromolecules, Collaborative Innovation Center of Chemistry for Life Sciences, School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230026, China
2Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, Anhui 230026, China
刊名: Biochemical and Biophysical Research Communications, 2017, Vol.494 (3-4), pp.575-580
来源数据库: Elsevier Journal
DOI: 10.1016/j.bbrc.2017.09.102
关键词: UHRF2PIP-boxPCNAStructureMolecular mechanism
英文摘要: Abstract(#br)UHRF2 (Ubiquitin-like with PHD and ring finger domains 2) is an E3 ubiquitin ligase that plays important roles in DNA methylation, histone modifications and cell cycle regulation by interacting with multiple epigenetic or cell-cycle related proteins. Previous studied have identified PCNA (Proliferating cell nuclear antigen) as an interacting partner of UHRF2 by using the antibody microarray. However, the molecular mechanism and the function of UHRF2-PCNA interaction remains unclear. Here, we report the complex structure of PCNA and the peptide ( 784 NEIL QTLLDLFF PGYSK 800 ) derived from UHRF2 that contains a PIP box. Structural analysis combined with mutagenesis experiments provide the molecular basis for the recognition of UHRF2 by PCNA via PIP-box.
全文获取路径: Elsevier  (合作)

  • interaction 相互酌
  • molecular 分子的
  • mechanism 机构
  • between 在中间