National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.
Crit Rev Biochem Mol Biol. 2013 May-Jun;48(3):211-21. doi: 10.3109/10409238.2012.742035. Epub 2012 Nov 27.
Proteins containing Bromo Adjacent Homology (BAH) domain are often associated with biological processes involving chromatin, and mutations in BAH domains have been found in human diseases. A number of structural and functional studies have revealed that the BAH domain plays diverse and versatile roles in chromatin biology, including protein-protein interactions, recognition of methylated histones and nucleosome binding. Here we review recent developments in structural studies of the BAH domain, and intend to place the structural results in the context of biological functions of the BAH domain-containing proteins. A converging theme from the structural studies appears that the predominantly β-sheet fold of the BAH domain serves as a scaffold, and function-specific structural features are incorporated at the loops connecting the β-strands and surface-exposed areas. The structures clearly specified regions critical for protein-protein interactions, located the position of methyllysine-binding site and implicated areas important for nucleosome binding. The structural results provided valuable insights into the molecular mechanisms of BAH domains in molecular recognitions, and the information should greatly facilitate mechanistic understanding of BAH domain proteins in chromatin biology.
含有溴相邻同源（BAH）结构域的蛋白质通常与涉及染色质的生物过程有关，并且在人类疾病中已经发现 BAH 结构域的突变。许多结构和功能研究表明，BAH 结构域在染色质生物学中发挥着多样化和通用的作用，包括蛋白-蛋白相互作用、识别甲基化组蛋白和核小体结合。在这里，我们回顾了 BAH 结构域结构研究的最新进展，并打算将结构结果置于 BAH 结构域蛋白的生物学功能背景下。结构研究的一个共同主题是，BAH 结构域主要的β-折叠作为一个支架，并且功能特异性的结构特征整合在连接β-链和表面暴露区域的环中。这些结构清楚地指定了对于蛋白-蛋白相互作用至关重要的区域，确定了甲基赖氨酸结合位点的位置，并暗示了对于核小体结合重要的区域。结构结果为 BAH 结构域在分子识别中的分子机制提供了有价值的见解，这些信息应该极大地促进对染色质生物学中 BAH 结构域蛋白的机制理解。
