Structural basis of the chromodomain of Cbx3 bound to methylated peptides from histone h1 and G9a.
作者: Jianbin RuanHui OuyangMaria F AmayaMani RavichandranPeter LoppnauJinrong MinJianye Zang
刊名: PLoS ONE, 2018, Vol.7 (4)
来源数据库: Directory of Open Access Journals
DOI: 10.1371/journal.pone.0035376
原始语种摘要: HP1 proteins are highly conserved heterochromatin proteins, which have been identified to be structural adapters assembling a variety of macromolecular complexes involved in regulation of gene expression, chromatin remodeling and heterochromatin formation. Much evidence shows that HP1 proteins interact with numerous proteins including methylated histones, histone methyltransferases and so on. Cbx3 is one of the paralogues of HP1 proteins, which has been reported to specifically recognize trimethylated histone H3K9 mark, and a consensus binding motif has been defined for the Cbx3 chromodomain.Here, we found that the Cbx3 chromodomain can bind to H1K26me2 and G9aK185me3 with comparable binding affinities compared to H3K9me3. We also determined the crystal structures of the human Cbx3...
全文获取路径: DOAJ  (合作)
影响因子:3.73 (2012)

  • histone 组蛋白
  • methylated 甲基化了的
  • proteins 蛋白质
  • expression 表示
  • basis 
  • chromatin 染色质
  • numerous 许多的
  • complex 超群
  • binding 装订
  • comparable 可比较的