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.