Preliminary crystallographic analysis of the RNA-binding domain of HuR and its poly(U)-binding properties.
Preliminary crystallographic analysis of the RNA-binding domain of HuR and its poly(U)-binding properties.
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DOI：
10.1107/s1744309110052930
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发表时间：
2011-05
期刊：
影响因子：
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通讯作者：
Hong Wang;Heng Li;Hui Shi;Yang Liu;Huihui Liu;Hui Zhao;L. Niu;M. Teng;Xu Li
中科院分区：
文献类型：
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作者：
Hong Wang;Heng Li;Hui Shi;Yang Liu;Huihui Liu;Hui Zhao;L. Niu;M. Teng;Xu Li
人类抗原 R (HuR) 是 Hu 蛋白家族中普遍表达的成员，是一种重要的转录后调节因子，具有三个 RNA 识别基序 (RRM) 结构域。两个串联的 N 端 RRM 结构域可以选择性地结合富含 AU 的元件 (ARE)，而第三个结构域则与 Poly(A) 尾部和其他蛋白质相互作用。在此，HuR 的重组 ARE 结合区（残基 18-186）在空间群 P2(1)2(1)2 中结晶，晶胞参数 a = 41.2、b = 133.1、c = 31.4 Å。收集分辨率为 2.8 Å 的 X 射线衍射数据。诱变分析和 SPR 测定揭示了其聚（U）结合特性。
Human antigen R (HuR), a ubiquitously expressed member of the Hu protein family, is an important post-transcriptional regulator which has three RNA-recognition motif (RRM) domains. The two tandem N-terminal RRM domains can selectively bind to the AU-rich element (ARE), while the third one interacts with the poly(A) tail and other proteins. Here, the recombinant ARE-binding region of HuR (residues 18-186) was crystallized in space group P2(1)2(1)2, with unit-cell parameters a = 41.2, b = 133.1, c = 31.4 Å. X-ray diffraction data were collected to a resolution of 2.8 Å. Mutagenesis analysis and SPR assays revealed its poly(U)-binding properties.