TY - JOUR
T1 - The complete primary structure of protein kinase C - The major phorbol ester receptor
AU - Parker, Peter J.
AU - Coussens, Lisa
AU - Totty, Nick
AU - Rhee, Lucy
AU - Young, Susan
AU - Chen, Ellson
AU - Stabel, Silvia
AU - Waterfield, Michael D.
AU - Ullrich, Axel
PY - 1986
Y1 - 1986
N2 - 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.
AB - 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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U2 - 10.1126/science.3755547
DO - 10.1126/science.3755547
M3 - Article
C2 - 3755547
AN - SCOPUS:0022545229
SN - 0036-8075
VL - 233
SP - 853
EP - 859
JO - Science
JF - Science
IS - 4766
ER -