8V9U
Solution NMR structure of human DNMT1 N-terminal alpha-helical domain
Summary for 8V9U
| Entry DOI | 10.2210/pdb8v9u/pdb |
| NMR Information | BMRB: 31134 |
| Descriptor | DNA (cytosine-5)-methyltransferase 1 (1 entity in total) |
| Functional Keywords | dnmt1, dna methylation, epigenetics, gene expression, transcription, dna damage repair, transferase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 9494.94 |
| Authors | Hu, Q.,Botuyan, M.V.,Mer, G. (deposition date: 2023-12-09, release date: 2024-02-28, Last modification date: 2024-06-05) |
| Primary citation | 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 Cited by 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: 38382673DOI: 10.1016/j.jbc.2024.105775 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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