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Science 22 August 1986:
Vol. 233. no. 4766, pp. 853 - 859
DOI: 10.1126/science.3755547
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Articles

Science, Vol 233, Issue 4766, 853-859
Copyright © 1986 by American Association for the Advancement of Science

articles

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

PJ Parker, L Coussens, N Totty, L Rhee, S Young, E Chen, S Stabel, MD Waterfield, and A Ullrich

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.


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