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Article

The PHD1 finger of KDM5B recognizes unmodified H3K4 during the demethylation of histone H3K4me2/3 by KDM5B.

Protein & cell - 1 Nov 2014

Zhang Yan, Yang Huirong, Guo Xue, Rong Naiyan, Song Yujiao, Xu Youwei, Lan Wenxian, Zhang Xu, Liu Maili, Xu Yanhui, Cao Chunyang

Abstract excerpt

KDM5B is a histone H3K4me2/3 demethylase. The PHD1 domain of KDM5B is critical for demethylation, but the mechanism underlying the action of this domain is unclear. In this paper, we observed that PHD1KDM5B interacts with unmethylated H3K4me0. Our NMR structure of PHD1KDM5B in complex with H3K4me0 revealed that the binding mode is slightly different from that of other reported PHD fingers. The disruption of this...

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Identifiers

PMID: 24952722
DOI: 10.1007/s13238-014-0078-4
PMCID: PMC4225485

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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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