Structural Insights into Histone Demethylation by JMJD2 Family Members
作者: Zhongzhou ChenJianye ZangJohnathan WhetstineXia HongFoteini DavrazouTatiana G. KutateladzeMichael SimpsonQilong MaoCheol-Ho PanShaodong DaiJames HagmanKirk HansenYang ShiGongyi Zhang
作者单位: 1Department of Immunology, National Jewish Medical and Research Center, Denver, CO 80206, USA
2Department of Pathology, Harvard Medical School, Boston, MA 02115, USA
3Department of Pharmacology and The Program in Biomolecular Structure, School of Medicine, University of Colorado Health Sciences Center, Denver, CO 80045, USA
4University of Colorado Cancer Center, Aurora, CO 80045, USA
刊名: Cell, 2006, Vol.125 (4), pp.691-702
来源数据库: Elsevier Journal
DOI: 10.1016/j.cell.2006.04.024
原始语种摘要: Summary(#br)Posttranslational modifications of histones regulate chromatin structure and gene expression. Histone demethylases, members of a newly emerging transcription-factor family, remove methyl groups from the lysine residues of the histone tails and thereby regulate the transcriptional activity of target genes. JmjC-domain-containing proteins have been predicted to be demethylases. For example, the JmjC-containing protein JMJD2A has been characterized as a H3-K9me3- and H3-K36me3-specific demethylase. Here, structures of the catalytic-core domain of JMJD2A with and without α -ketoglutarate in the presence of Fe 2+ have been determined by X-ray crystallography. The structure of the core domain, consisting of the JmjN domain, the JmjC domain, the C-terminal domain, and a zinc-finger...
全文获取路径: Elsevier  (合作)
影响因子:31.957 (2012)

  • domain 领域
  • proteins 蛋白质
  • chromatin 染色质
  • mutagenesis 突变形成
  • expression 表示
  • family 
  • ketoglutarate 酮戊二酸盐或酯
  • allowed 容许
  • remove 除去
  • regulate 控制