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首页> 外文期刊>Journal of Molecular Biology >THREE-DIMENSIONAL STRUCTURE OF MAMMALIAN CASEIN KINASE I - MOLECULAR BASIS FOR PHOSPHATE RECOGNITION
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THREE-DIMENSIONAL STRUCTURE OF MAMMALIAN CASEIN KINASE I - MOLECULAR BASIS FOR PHOSPHATE RECOGNITION

机译：哺乳动物酪蛋白激酶I的三维结构-磷酸盐识别的分子基础。

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摘要

The three-dimensional structure for the catalytic region of the mammalian protein kinase, casein kinase I delta (CKI delta), has been solved by X-ray crystallography to a resolution of 2.3 Angstrom. A truncation mutant of CKI delta lacking the C-terminal autoinhibitory region was expressed in Escherichia coli, purified, and crystallized. The structure was solved by molecular replacement using the crystal structure of the catalytic domain of a CKI homolog from Schizosaccharomyces pombe, Cki1. A tungstate derivative confirmed the initial molecular replacement solution and identified an anion binding site which may contribute to the unique substrate specificity of CKI. Like other protein kinases, the catalytic domain of CKI is composed of two lobes with a cleft between them for binding ATP. Comparison of the mammalian and yeast CKI structures suggests that a rotation of the N-terminal domain occurs upon ATP binding. This domain motion is similar, but not identical, to that observed in cAMP-dependent protein kinase upon binding ATP. Although Cki1 has many similarities to CKI delta over the catalytic domain, these two forms of CKI likely perform different functions in vivo. Relating the primary sequences of other CKI enzymes to the three-dimensional architecture of CKI delta reveals a catalytic face that is especially conserved among the subset of CKI family members associated with the regulation of DNA repair. (C) 1996 Academic Press Limited [References: 56]
机译：哺乳动物蛋白激酶（酪蛋白激酶Iδ）（CKIδ）催化区域的三维结构已通过X射线晶体学解析为2.3埃的分辨率。缺乏C端自抑制区的CKIδ截短突变体在大肠杆菌中表达，纯化和结晶。通过分子置换，使用来自粟酒裂殖酵母（Schizosaccharomyces pombe）Cki1的CKI同源物催化域的晶体结构来解决结构。钨酸盐衍生物证实了最初的分子置换溶液，并确定了可能有助于CKI独特底物特异性的阴离子结合位点。像其他蛋白激酶一样，CKI的催化结构域由两个裂片组成，它们之间有一个裂口，用于结合ATP。哺乳动物和酵母CKI结构的比较表明，N末端结构域的旋转在ATP结合时发生。该域运动与结合ATP后在cAMP依赖性蛋白激酶中观察到的相似但不相同。尽管Cki1在催化域上与CKIδ有许多相似之处，但是这两种形式的CKI在体内可能执行不同的功能。将其他CKI酶的一级序列与CKI三角洲的三维结构相关联，揭示出催化面，在与DNA修复调控相关的CKI家族成员子集中尤其保守。 （C）1996 Academic Press Limited [参考号：56]

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