Solution structure of BRD7 bromodomain and its interaction with acetylated peptides from histone H3 and H4
作者： Hongbin Sun , Jiangxin Liu , Jiahai Zhang , Weiqun Shen , Hongda Huang
DOI: 10.1016/J.BBRC.2007.04.139
关键词:
摘要: BRD7 is an important protein tightly associated with Nasopharyngeal carcinoma (NPC). Overexpression of inhibits NPC cell growth and cycle by transcriptionally regulating the related genes. contains a bromodomain that found in many chromatin-associated proteins nearly all known nuclear histone acetyltransferases (HATs) plays role chromatin remodeling transcriptional activation. Here, we report solution structure determined NMR spectroscopy, its binding specificity revealed titration several acetylated peptides. We find typical left-handed four-helix bundle topology, can bind weak affinity to lysine-acetylated peptides derived from H3 K9 or K14 H4 K8, K12 K16 acetylated. Our results show lacks inherent when histones vitro.
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