一种可磷酸化tau蛋白的人tau-微管蛋白激酶2的表达、纯化及结晶
Expression, purification and crystallization of a human tau-tubulin kinase 2 that phosphorylates tau protein.
作者信息
Kitano-Takahashi Michiko, Morita Hiroyuki, Kondo Shin, Tomizawa Kayoko, Kato Ryohei, Tanio Michikazu, Shirota Yoshiko, Takahashi Hiroshi, Sugio Shigetoshi, Kohno Toshiyuki
机构信息
Mitsubishi Kagaku Institute of Life Sciences, 11 Minamiooya, Machida, Tokyo 194-8511, Japan.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jul 1;63(Pt 7):602-4. doi: 10.1107/S1744309107028783. Epub 2007 Jun 15.
Abstract
Tau-tubulin kinase 2 (TTBK2) is a Ser/Thr kinase that putatively phosphorylates residues Ser208 and Ser210 (numbered according to a 441-residue human tau isoform) in tau protein. Functional analyses revealed that a recombinant kinase domain (residues 1-331) of human TTBK2 expressed in insect cells with a baculovirus overexpression system retains kinase activity for tau protein. The kinase domain of TTBK2 was crystallized using the hanging-drop vapour-diffusion method. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 55.6, b = 113.7, c = 117.3 A, alpha = beta = gamma = 90.0 degrees. Diffraction data were collected to 2.9 A resolution using synchrotron radiation at BL24XU of SPring-8.
摘要
微管相关蛋白tau的蛋白激酶2（TTBK2）是一种丝氨酸/苏氨酸激酶，可能使tau蛋白中的丝氨酸208和丝氨酸210位点（根据441个氨基酸残基的人tau异构体编号）发生磷酸化。功能分析表明，利用杆状病毒过表达系统在昆虫细胞中表达的人TTBK2重组激酶结构域（氨基酸残基1 - 331）保留了对tau蛋白的激酶活性。采用悬滴气相扩散法对TTBK2的激酶结构域进行了结晶。晶体属于空间群P2(1)2(1)2(1)，晶胞参数为a = 55.6，b = 113.7，c = 117.3 Å，α = β = γ = 90.0°。使用日本理化学研究所八重洲同步加速器BL24XU的同步辐射收集了分辨率为2.9 Å的衍射数据。
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