3DWH

Structural and Functional Analysis of SRA domain

3DWH の概要

• エントリーDOI: 10.2210/pdb3dwh/pdb
• 分子名称: E3 ubiquitin-protein ligase UHRF1, SULFATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: beta barrel, cell cycle, dna damage, dna repair, dna-binding, ligase, metal-binding, nucleus, phosphoprotein, transcription, transcription regulation, ubl conjugation pathway, zinc-finger
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Nucleus: Q96T88
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23436.09

構造登録者

Qian, C.,Jakoncic, J.,Zhou, M. (登録日: 2008-07-22, 公開日: 2008-10-21, 最終更新日: 2024-03-13)

主引用文献

Qian, C.,Li, S.,Jakoncic, J.,Zeng, L.,Walsh, M.J.,Zhou, M.M.
Structure and Hemimethylated CpG Binding of the SRA Domain from Human UHRF1.
J.Biol.Chem., 283:34490-34494, 2008

PubMed Abstract: Human UHRF1 (ubiquitin-like PHD and RING finger 1) functions to maintain CpG DNA methylation patterns through DNA replication by co-localizing with the DNA methyltransferase DNMT1 at chromatin in mammals. Recent studies show that UHRF1 binds selectively to hemimethylated CpG via its conserved SRA (SET- and RING finger-associated) domain. However, the underlying molecular mechanism is not known. Here, we report a 1.95 A resolution crystal structure of the SRA domain of human UHRF1. Using NMR structure-guided mutagenesis, electrophoretic mobility shift assay, and fluorescence anisotropy analysis, we determined key amino acid residues for methyl-DNA binding that are conserved in the SRA domain.

PubMed: 18945682
DOI: 10.1074/jbc.C800169200

実験手法

X-RAY DIFFRACTION (1.95 Å)