8V9U

Solution NMR structure of human DNMT1 N-terminal alpha-helical domain

8V9U の概要

• エントリーDOI: 10.2210/pdb8v9u/pdb
• NMR情報: BMRB: 31134
• 分子名称: DNA (cytosine-5)-methyltransferase 1 (1 entity in total)
• 機能のキーワード: dnmt1, dna methylation, epigenetics, gene expression, transcription, dna damage repair, transferase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9494.94

構造登録者

Hu, Q.,Botuyan, M.V.,Mer, G. (登録日: 2023-12-09, 公開日: 2024-02-28, 最終更新日: 2024-06-05)

主引用文献

Hu, Q.,Botuyan, M.V.,Mer, G.
Identification of a conserved alpha-helical domain at the N terminus of human DNA methyltransferase 1.
J.Biol.Chem., 300:105775-105775, 2024

PubMed Abstract: In vertebrates, DNA methyltransferase 1 (DNMT1) contributes to preserving DNA methylation patterns, ensuring the stability and heritability of epigenetic marks important for gene expression regulation and the maintenance of cellular identity. Previous structural studies have elucidated the catalytic mechanism of DNMT1 and its specific recognition of hemimethylated DNA. Here, using solution nuclear magnetic resonance spectroscopy and small-angle X-ray scattering, we demonstrate that the N-terminal region of human DNMT1, while flexible, encompasses a conserved globular domain with a novel α-helical bundle-like fold. This work expands our understanding of the structure and dynamics of DNMT1 and provides a structural framework for future functional studies in relation with this new domain.

PubMed: 38382673
DOI: 10.1016/j.jbc.2024.105775

実験手法

SOLUTION NMR