Parker P J, Coussens L, Totty N, Rhee L, Young S, Chen E, Stabel S, Waterfield M D, Ullrich A
Science. 1986 Aug 22;233(4766):853-9. doi: 10.1126/science.3755547.
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.
蛋白激酶C是主要的佛波酯受体,它从牛脑中纯化得到,通过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,揭示了一种结构域结构。在氨基末端是一个富含半胱氨酸的结构域,内部有重复序列;接着是一个假定的钙结合结构域,在羧基末端有一个与其他蛋白激酶序列有显著同源性但不完全相同的结构域。