富含腺苷酸/尿苷酸元件结合蛋白HuR与其靶RNA复合物的克隆、表达、纯化及初步晶体学研究。
Cloning, expression, purification and preliminary crystallographic studies of the adenylate/uridylate-rich element-binding protein HuR complexed with its target RNA.
作者信息
Iyaguchi Daisuke, Yao Min, Tanaka Isao, Toyota Eiko
机构信息
Health Sciences University of Hokkaido, Japan.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Mar 1;65(Pt 3):285-7. doi: 10.1107/S174430910900400X. Epub 2009 Feb 26.
Abstract
Adenylate/uridylate-rich elements (AREs), which are found in the 3'-untranslated region (UTR) of many mRNAs, influence the stability of cytoplasmic mRNA. HuR (human antigen R) binds to AREs and regulates various genes. In order to reveal the RNA-recognition mechanism of HuR protein, an RNA-binding region of human HuR containing two N-terminal RNA-recognition motif domains bound to an 11-base RNA fragment has been crystallized. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 42.4, b = 44.9, c = 91.1 A. X-ray diffraction data were collected to 1.8 A resolution.
摘要
富含腺苷酸/尿苷酸元件（AREs）存在于许多mRNA的3'非翻译区（UTR）中，影响细胞质mRNA的稳定性。HuR（人类抗原R）与AREs结合并调控多种基因。为了揭示HuR蛋白的RNA识别机制，包含两个N端RNA识别基序结构域的人类HuR的一个RNA结合区域已与一个11碱基的RNA片段结合并结晶。晶体属于空间群P2(1)2(1)2(1)，晶胞参数a = 42.4，b = 44.9，c = 91.1 Å。X射线衍射数据收集至1.8 Å分辨率。
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