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Article

Structural insight into hierarchical DNMT3A autoinhibition and its dysregulation in disease.

Nature communications - 18 Feb 2026

Lu Jiuwei, Vig Emily, Chen Jianbin, Gretarsson Kristjan H, Khudaverdyan Nelli, Shao Zengyu, Lu Chao, Chang Chia-En A, Song Jikui

Abstract excerpt

DNA methyltransferase DNMT3A-mediated DNA methylation is important for genomic imprinting and transcriptional regulation. However, how the regulatory domains of DNMT3A cooperate with its methyltransferase domain and histone marks to orchestrate genomic methylation remains unclear. Here we report the cryo-EM structure of DNMT3A2 with regulatory factor DNMT3L, revealing an intricate domain interaction underlying...

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Share to Allosteric Regulation
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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 41708613
DOI: 10.1038/s41467-026-69563-1
PMCID: PMC13031684

Genes

DNMT3A
DNMT3L

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 20 Oct 2026.

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