A NOVEL PROTEIN-KINASE WITH LEUCINE ZIPPER-LIKE SEQUENCES - ITS CATALYTIC DOMAIN IS HIGHLY HOMOLOGOUS TO THAT OF PROTEIN-KINASE-C
A NOVEL PROTEIN-KINASE WITH LEUCINE ZIPPER-LIKE SEQUENCES - ITS CATALYTIC DOMAIN IS HIGHLY HOMOLOGOUS TO THAT OF PROTEIN-KINASE-C
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DOI：
10.1006/bbrc.1994.1313
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发表时间：
1994-03-15
影响因子：
3.1
通讯作者：
ONO, Y
中科院分区：
文献类型：
--
作者：
MUKAI, H;ONO, Y
利用分子克隆技术，从人海马cDNA文库中鉴定出一种新的蛋白激酶PKN。PKN由942个氨基酸组成，计算的分子质量为103,925道尔顿。PKN在其氨基末端具有亮氨酸拉链状序列，并且包含一个与蛋白激酶C家族具有很强相似性的催化结构域。Northern blot分析表明PKN在人体组织中普遍表达。当PKN在昆虫细胞或COS7细胞中表达时，抗PKN血清经SDS聚丙烯酰胺凝胶电泳鉴定为120K道尔顿蛋白。重组PKN显示了与120K蛋白相关的内在蛋白激酶活性。这种活性被潜在ATP结合位点赖氨酸残基的突变所消除。(C) 1994学术出版社，Inc.
A novel protein kinase, designated PKN, was identified by molecular cloning from a human hippocampus cDNA library. PKN consists of 942 amino acids with a calculated molecular mass of 103,925 daltons. PKN has leucine zipper-like sequences in its amino terminal region and contains a catalytic domain that shows strong similarity to that of protein kinase C family. Northern blot analysis indicates PKN is expressed ubiquitously in human tissues. Antisera against PKN identified a 120K dalton protein on SDS polyacrylamide gel electrophoresis when PKN was expressed in the insect cells or COS7 cells. Recombinant PKN revealed an intrinsic protein kinase activity associated with a 120K protein. This activity was abolished by mutation of the lysine residue in the potential ATP binding site. (C) 1994 Academic Press, Inc.