Cooperative binding of two acetylation marks on a histone tail by a single bromodomain
Cooperative binding of two acetylation marks on a histone tail by a single bromodomain
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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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Histone modification: tail spin
Brdt1 is a bromodomain-containing chromatin protein that can compact hyperacetylated chromatin and has important functions during spermiogenesis. Here, the crystal structure of a bromodomain of Brdt1 bound to an acetylated histone H4 tail reveals a combinatorial mode of binding to post-translational modifications...
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Cooperative binding of two acetylation marks on a histone tail by a single bromodomain
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TN_cdi_hal_primary_oai_HAL_cea_00909643v1
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_hal_primary_oai_HAL_cea_00909643v1
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ISSN
0028-0836,1743-4378
E-ISSN
1476-4687,1743-4386
DOI
10.1038/nature08397
