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Article

Structural Insights into Histone Crotonyl-Lysine Recognition by the AF9 YEATS Domain.

Structure (London, England : 1993) - 6 Sept 2016

Zhang Qiang, Zeng Lei, Zhao Chengcheng, Ju Ying, Konuma Tsuyoshi, Zhou Ming-Ming

Abstract excerpt

Histone lysine acylations play an important role in the regulation of gene transcription in chromatin. Unlike histone acetyl-lysine, molecular recognition of a recently identified crotonyl-lysine mark is much less understood. Here, we report that the YEATS domain of AF9 preferentially binds crotonyl-lysine over acetyl-lysine in histone H3. Nuclear magnetic resonance structural analysis reveals that...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 27545619
DOI: 10.1016/j.str.2016.05.023
PMCID: PMC5014688

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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