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HuR的RNA结合结构域的初步晶体学分析及其与聚尿苷的结合特性。

Preliminary crystallographic analysis of the RNA-binding domain of HuR and its poly(U)-binding properties.

作者信息

Wang Hong, Li Heng, Shi Hui, Liu Yang, Liu Huihui, Zhao Hui, Niu Liwen, Teng Maikun, Li Xu

机构信息

Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, People's Republic of China.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 May 1;67(Pt 5):546-50. doi: 10.1107/S1744309110052930. Epub 2011 Apr 21.

Abstract

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.

摘要

人抗原R(HuR)是Hu蛋白家族中一种广泛表达的成员,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与富含AU元件(ARE)结合,而第三个结构域则与聚腺苷酸尾和其他蛋白质相互作用。在此,HuR的重组ARE结合区域(第18 - 186位氨基酸残基)在空间群P2(1)2(1)2中结晶,晶胞参数为a = 41.2,b = 133.1,c = 31.4 Å。X射线衍射数据收集到2.8 Å的分辨率。诱变分析和表面等离子体共振(SPR)测定揭示了其与聚尿苷酸(poly(U))的结合特性。

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Identification of a target RNA motif for RNA-binding protein HuR.RNA结合蛋白HuR的靶RNA基序的鉴定
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