Identification of a new class of protein kinases represented by eukaryotic elongation factor-2 kinase
Identification of a new class of protein kinases represented by eukaryotic elongation factor-2 kinase
复制标题
鉴定以真核生物伸长因子-2激酶为代表的一类新型蛋白激酶
DOI：
10.1073/pnas.94.10.4884
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发表时间：
1997-05-13
影响因子：
11.1
通讯作者：
Hait, WN
中科院分区：
文献类型：
--
作者：
Ryazanov, AG;Ward, MD;Hait, WN
到目前为止，真核蛋白激酶超家族的数百个成员具有相似的催化结构域结构，由12个保守的亚域组成。本文报道了一种结构完全不同的蛋白激酶在真核生物中的广泛存在。我们克隆并测定了人、小鼠、大鼠和秀丽线虫真核延伸因子-2激酶(EEF-2)的序列，发现除了与ATP结合的部位外，它们不包含任何具有真核蛋白激酶超家族特征的序列基序。比较不同的EEF-2激酶序列，发现有一个约200个氨基酸的高度保守的区域，与最近从网柄菌中发现的肌球蛋白重链激酶A(MHCK A)的催化结构域同源。这表明EEF-2和MHCK A是一类新的具有催化结构域结构的蛋白激酶成员。
The several hundred members of the eukaryotic protein kinase superfamily characterized to date share a similar catalytic domain structure, consisting of 12 conserved subdomains. Here we report the existence and wide occurrence in eukaryotes of a protein kinase with a completely different structure, We cloned and sequenced the human, mouse, rat, and Caenorhabditis elegans eukaryotic elongation factor-2 kinase (eEF-2 kinase) and found that with the exception of the ATP-binding site, they do not contain any sequence motifs characteristic of the eukaryotic protein kinase superfamily, Comparison of different eEF-2 kinase sequences reveals a highly conserved region of approximate to 200 amino acids which was found to be homologous to the catalytic domain of the recently described myosin heavy chain kinase A (MHCK A) from Dictyostelium. This suggests that eEF-2 kinase and MHCK A are members of a new class of protein kinases with a novel catalytic domain structure.