Protein kinase CK2: From structures to insights
Protein kinase CK2: From structures to insights
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DOI：
10.1007/s00018-009-9149-8
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发表时间：
2009-06-01
影响因子：
8
通讯作者：
Issinger, O. -G.
中科院分区：
文献类型：
--
作者：
Niefind, K.;Raaf, J.;Issinger, O. -G.
在过去的十年中，发表了40种对应于蛋白激酶CK 2（以前的名称为“酪蛋白激酶2”）、其催化亚基CK 2 α和其调节亚基CK 2 β的晶体结构。它们一起提供了一个有价值的，但到目前为止还不完整的基础，合理化酶的生化特征，如其组成活性，嗜酸性底物特异性，双辅底物特异性和其异四聚体的四元结构。结构叠加的综合组揭示了CK 2 α和CK 2 β都是相对刚性的分子。在CK 2 β中，CK 2 α募集的关键区域在未结合状态下预先形成。在CK 2 α中，激活片段-蛋白激酶调节的关键元件-总是适应活性酶的典型构象。人类CK 2 α的最新结构揭示了ATP结合区令人惊讶的可塑性，表明了另一种活性控制模式。(Part多作者评论）
Within the last decade, 40 crystal structures corresponding to protein kinase CK2 (former name 'casein kinase 2'), to its catalytic subunit CK2 alpha and to its regulatory subunit CK2 beta were published. Together they provide a valuable, yet by far not complete basis to rationalize the biochemical features of the enzyme, such as its constitutive activity, acidophilic substrate specificity, dual-cosubstrate specificity and its heterotetrameric quarternary structure. Comprehensive sets of structural superimpositions reveal that both CK2 alpha and CK2 beta are relatively rigid molecules. In CK2 beta the critical region of CK2 alpha recruitment is pre-formed in the unbound state. In CK2 alpha the activation segment-a key element of protein kinase regulation-adapts invariably the typical conformation of the active enzymes. Recent structures of human CK2 alpha revealed a surprising plasticity in the ATP-binding region, suggesting an alternative mode of activity control. (Part of a Multi-author Review)