Structural insights into the π-π-π stacking mechanism and DNA-binding activity of the YEATS domain
Structural insights into the π-π-π stacking mechanism and DNA-binding activity of the YEATS domain
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London: Nature Publishing Group UK
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English
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London: Nature Publishing Group UK
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The YEATS domain has been identified as a reader of histone acylation and more recently emerged as a promising anti-cancer therapeutic target. Here, we detail the structural mechanisms for π-π-π stacking involving the YEATS domains of yeast Taf14 and human AF9 and acylated histone H3 peptides and explore DNA-binding activities of these domains. Taf...
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Structural insights into the π-π-π stacking mechanism and DNA-binding activity of the YEATS domain
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TN_cdi_doaj_primary_oai_doaj_org_article_0a782d5b6bf841aea5a1f2ccefd9b04c
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_0a782d5b6bf841aea5a1f2ccefd9b04c
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ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-018-07072-6
