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PDBsum entry 2dvr
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Transcription
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PDB id
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2dvr
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References listed in PDB file
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Key reference
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Title
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Structural basis for acetylated histone h4 recognition by the human brd2 bromodomain.
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Authors
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T.Umehara,
Y.Nakamura,
M.K.Jang,
K.Nakano,
A.Tanaka,
K.Ozato,
B.Padmanabhan,
S.Yokoyama.
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Ref.
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J Biol Chem, 2010,
285,
7610-7618.
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PubMed id
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Abstract
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Recognition of acetylated chromatin by the bromodomains and extra-terminal
domain (BET) family proteins is a hallmark for transcriptional activation and
anchoring viral genomes to mitotic chromosomes of the host. One of the BET
family proteins BRD2 interacts with acetylated chromatin during mitosis and
leads to transcriptional activation in culture cells. Here, we report the
crystal structures of the N-terminal bromodomain of human BRD2 (BRD2-BD1;
residues 74-194) in complex with each of three different Lys-12-acetylated H4
peptides. The BRD2-BD1 recognizes the H4 tail acetylated at Lys-12 (H4K12ac),
whereas the side chain of hypoacetylated Lys-8 of H4 binds at the cavity of the
dimer interface of BRD2-BD1. From binding studies, we identified the BRD2-BD1
residues that are responsible for recognition of the Lys-12-acetylated H4 tail.
In addition, mutation to Lys-8 in the Lys-12-acetylated H4 tail decreased the
binding to BRD2-BD1, implicating the critical role of Lys-8 in the
Lys-12-acetylated H4 tail for the recognition by BRD2-BD1. Our findings provide
a structural basis for deciphering the histone code by the BET bromodomain
through the binding with a long segment of the histone H4 tail, which presumably
prevents erasure of the histone code during the cell cycle.
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