THE COMPLETE PRIMARY STRUCTURE OF PROTEIN-KINASE-C - THE MAJOR PHORBOL ESTER RECEPTOR
THE COMPLETE PRIMARY STRUCTURE OF PROTEIN-KINASE-C - THE MAJOR PHORBOL ESTER RECEPTOR
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DOI：
10.1126/science.3755547
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发表时间：
1986-08-22
期刊：
影响因子：
56.9
通讯作者：
ULLRICH, A
中科院分区：
文献类型：
--
作者：
PARKER, PJ;COUSSENS, L;ULLRICH, A
从牛脑中纯化了主要的酚酯受体蛋白激酶C，利用基于部分氨基酸序列的寡核苷酸探针，从牛脑互补DNA文库中获得了互补DNA克隆。因此，确定了牛蛋白激酶C的完整氨基酸序列，揭示了其结构域结构。在氨基端是一个富含半胱氨酸的结构域，具有内部重复；随后是一个假定的钙结合结构域，在羧基末端有一个结构域，与其他蛋白激酶的序列显示出实质性的同源性，但不是同一性。
Protein kinase C, the major phorbol ester receptor, was purified from bovine brain and through the use of oligonucleotide probes based on partial amino acid sequence, complementary DNA clones were derived from bovine brain complementary DNA libraries. Thus, the complete amino acid sequence of bovine protein kinase C was determined, revealing a domain structure. At the amino terminal is a cysteine-rich domain with an internal duplication; a putative calcium-binding domain follows, and there is at the carboxyl terminal a domain that shows substantial homology, but not identity, to sequences of other protein kinase.