Resonance assignments for the tandem PWWP-ARID domains of human RBBP1
Resonance assignments for the tandem PWWP-ARID domains of human RBBP1
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DOI：
10.1007/s12104-019-09873-2
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发表时间：
2019-01
影响因子：
0.9
通讯作者：
Weibin Gong;X. Yao;Qihui Liang;Y. Tong;S. Perrett;Yingang Feng
中科院分区：
文献类型：
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作者：
Weibin Gong;X. Yao;Qihui Liang;Y. Tong;S. Perrett;Yingang Feng
视网膜母细胞瘤结合蛋白1（RBBP 1），也称为AT丰富的相互作用结构域4A（ARID 4A），是一种肿瘤抑制因子，参与白血病和Prader-Willi/Angelman综合征的表观遗传编程的调节。RBBP 1的ARID结构域与DNA非特异性结合，具有基因抑制活性。然而，迄今为止还没有获得人RBBP 1 ARID结构域的结构数据。在这里，我们报告了一个27 kDa的串联PWWP-ARID结构域构建体，跨越残基171-414，去除两个结构域之间的一个短的无序区域的近完整的1H，13 C，15 N骨架和侧链NMR分配。基于分配的化学位移的预测的二级结构与先前解决的人RBBP 1的分离的PWWP结构域和其他蛋白质的同源ARID结构域的结构一致。
Retinoblastoma-binding protein 1 (RBBP1), also known as AT-rich interaction domain 4A (ARID4A), is a tumour suppressor involved in the regulation of the epigenetic programming in leukemia and Prader-Willi/Angelman syndromes. The ARID domain of RBBP1 binds to DNA non-specifically and has gene suppression activity. However, no structural data has been obtained for the human RBBP1 ARID domain so far. Here we report the near-complete1H,13C,15N backbone and side-chain NMR assignment of a 27 kDa tandem PWWP-ARID domain construct that spans residues 171–414 with the removal of a short disordered region between the two domains. The predicted secondary structure based on the assigned chemical shifts is consistent with the structures of the isolated PWWP domain of human RBBP1 previously solved and the homologous ARID domains of other proteins.