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Article

Crystal structures of the human histone H4K20 methyltransferases SUV420H1 and SUV420H2.

FEBS letters - 29 Nov 2013

Wu Hong, Siarheyeva Alena, Zeng Hong, Lam Robert, Dong Aiping, Wu Xian-Hui, Li Yanjun, Schapira Matthieu, Vedadi Masoud, Min Jinrong

Abstract excerpt

SUV420H1 and SUV420H2 are two highly homologous enzymes that methylate lysine 20 of histone H4 (H4K20), a mark that has been implicated in transcriptional regulation. In this study, we present the high-resolution crystal structures of human SUV420H1 and SUV420H2 in complex with SAM, and report their substrate specificity. Both methyltransferases have a unique N-terminal domain and Zn-binding post-SET domain, and...

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Share to Crystallography, X-Ray
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 24396869
DOI: 10.1016/j.febslet.2013.10.020

Genes

SET

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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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