人磷酸二酯酶12的结晶及初步X射线晶体学分析
Crystallization and preliminary X-ray crystallographic analysis of human phosphodiesterase 12.
作者信息
Kohno Tetsuya, Yamaguchi Hiroto, Hakoshima Toshio
机构信息
Structural Biology Laboratory, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 May 1;66(Pt 5):520-2. doi: 10.1107/S1744309110008766. Epub 2010 Apr 29.
Abstract
Phosphodiesterase PDE12 is a medically important esterase-family member that hydrolyzes 2'-5'-linked oligoadenylates (2-5A), which are involved in the regulation of biological processes related to the antiviral and antitumour activity that can be induced by interferons. Here, cloning, purification and crystallization of the C-terminal endonuclease/exonuclease/phosphatase-homology domain of human PDE12 is reported. The crystals belonged to space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 111.3, c = 192.4 A, and diffracted to 2.5 A resolution. Assuming the presence of three molecules in the asymmetric unit, the solvent content was estimated to be about 44.0%.
摘要
磷酸二酯酶PDE12是一种具有重要医学意义的酯酶家族成员，它能水解2'-5'-连接的寡腺苷酸（2-5A），这些寡腺苷酸参与了与抗病毒和抗肿瘤活性相关的生物过程的调节，而这些活性可由干扰素诱导产生。在此，报道了人PDE12 C末端核酸内切酶/核酸外切酶/磷酸酶同源结构域的克隆、纯化和结晶。晶体属于空间群P3(1)21或P3(2)21，晶胞参数a = b = 111.3，c = 192.4 Å，衍射分辨率达到2.5 Å。假设不对称单位中有三个分子，溶剂含量估计约为44.0%。
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