Publication Date:
1986-08-22
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Parker, P J -- Coussens, L -- Totty, N -- Rhee, L -- Young, S -- Chen, E -- Stabel, S -- Waterfield, M D -- Ullrich, A -- New York, N.Y. -- Science. 1986 Aug 22;233(4766):853-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3755547" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Animals
;
Brain/metabolism
;
*Caenorhabditis elegans Proteins
;
Carrier Proteins
;
Cattle
;
Dna
;
Models, Chemical
;
Protein Biosynthesis
;
*Protein Kinase C/isolation & purification
;
RNA, Messenger/metabolism
;
*Receptors, Drug
;
*Receptors, Immunologic
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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