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PDBsum entry 2i7k
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Transcription
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PDB id
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2i7k
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References listed in PDB file
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Key reference
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Title
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Solution structure of brd7 bromodomain and its interaction with acetylated peptides from histone h3 and h4.
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Authors
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H.Sun,
J.Liu,
J.Zhang,
W.Shen,
H.Huang,
C.Xu,
H.Dai,
J.Wu,
Y.Shi.
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Ref.
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Biochem Biophys Res Commun, 2007,
358,
435-441.
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PubMed id
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Abstract
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BRD7 is an important protein tightly associated with Nasopharyngeal carcinoma
(NPC). Overexpression of BRD7 inhibits NPC cell growth and cell cycle by
transcriptionally regulating the cell cycle related genes. BRD7 contains a
bromodomain that is found in many chromatin-associated proteins and in nearly
all known nuclear histone acetyltransferases (HATs) and plays an important role
in chromatin remodeling and transcriptional activation. Here, we report the
solution structure of BRD7 bromodomain determined by NMR spectroscopy, and its
binding specificity revealed by NMR titration with several acetylated histone
peptides. We find that BRD7 bromodomain contains the typical left-handed
four-helix bundle topology, and can bind with weak affinity to lysine-acetylated
peptides derived from histone H3 with K9 or K14 acetylated and from histone H4
with K8, K12 or K16 acetylated. Our results show that BRD7 bromodomain lacks
inherent binding specificity when binding to histones in vitro.
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