溴尿嘧啶
染色质
瑞士/瑞士法郎
蛋白质结构域
DNA结合域
生物
化学
核蛋白
细胞生物学
染色质重塑
计算生物学
遗传学
DNA
组蛋白
转录因子
基因
作者
Antony W. Oliver,Sarah Jones,S. Mark Roe,Stephen Matthews,Graham H. Goodwin,Laurence H. Pearl
摘要
The BAH domain (bromo-associated homology domain) was first identified from a repeated motif found in the nuclear protein polybromo--a large (187 kDa) modular protein comprising six bromodomains, two BAH domains and an HMG box. To date, the BAH domain has no ascribed function, although it is found in a wide range of proteins that contain additional domains involved in either transcriptional regulation (e.g. SET, PHD and bromodomain) and/or DNA binding (HMG box and AT hook). The molecular function of polybromo itself also remains unclear, but it has been identified as a key component of an SWI/SNF (switching/sucrose non-fermenting)-related, ATP-dependent chromatin-remodelling complex PBAF (polybromo, BRG1-associated factors; also known as SWI/SNF-B or SWI/SNFbeta). We present in this paper the crystal structure of the proximal BAH domain from chicken polybromo (BAH1), at a resolution of 1.6 A (1 A=0.1 nm). Structure-based sequence analysis reveals several features that may be involved in mediating protein-protein interactions.
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