Department of Integrative Structural and Computational Biology and Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
FEBS Lett. 2013 Aug 19;587(16):2506-11. doi: 10.1016/j.febslet.2013.06.051. Epub 2013 Jul 4.
The transcriptional co-regulator CBP (CREB-binding protein) has a highly conserved cysteine/histidine-rich region (CH2) whose structure and function remain uncharacterized. Using nuclear magnetic resonance (NMR spectroscopy), sequence alignment, mass spectrometry, and mutagenesis, we show that the CH2 domain is not a canonical plant homeodomain (PHD) finger, as previously proposed, but binds an additional zinc atom through the region N-terminal to the putative PHD motif. The CH2 domain and the preceding bromodomain interact and mutually stabilize each other, implying a cooperative function. We tested the hypothesis that the bromodomain and the CH2 domain can interact with histones, but found that the CH2 does not participate in histone-recognition.
转录共调节因子 CBP（CREB 结合蛋白）具有高度保守的半胱氨酸/组氨酸丰富区域（CH2），但其结构和功能仍未被阐明。我们使用核磁共振（NMR 光谱）、序列比对、质谱分析和突变分析表明，CH2 结构域不是先前提出的经典植物同源结构域（PHD）指，而是通过假定 PHD 基序的 N 端区域结合额外的锌原子。CH2 结构域和前面的溴结构域相互作用并相互稳定，暗示着协同功能。我们测试了溴结构域和 CH2 结构域是否可以与组蛋白相互作用的假设，但发现 CH2 不参与组蛋白识别。
