The complete primary structure of protein kinase C - The major phorbol ester receptor

Peter J. Parker, Lisa Coussens, Nick Totty, Lucy Rhee, Susan Young, Ellson Chen, Silvia Stabel, Michael D. Waterfield, Axel Ullrich

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Abstract

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.

Original languageEnglish (US)
Pages (from-to)853-859
Number of pages7
JournalScience
Volume233
Issue number4766
DOIs
StatePublished - Jan 1 1986

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    Parker, P. J., Coussens, L., Totty, N., Rhee, L., Young, S., Chen, E., Stabel, S., Waterfield, M. D., & Ullrich, A. (1986). The complete primary structure of protein kinase C - The major phorbol ester receptor. Science, 233(4766), 853-859. https://doi.org/10.1126/science.3755547