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

Research output: Contribution to journalArticle

575 Citations (Scopus)

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
StatePublished - 1986
Externally publishedYes

Fingerprint

Protein Kinase C
Amino Acid Sequence
Complementary DNA
Oligonucleotide Probes
Brain
Gene Library
Protein Kinases
Cysteine
Clone Cells
Calcium
phorbol ester receptor

ASJC Scopus subject areas

  • General

Cite this

Parker, P. J., Coussens, L., Totty, N., Rhee, L., Young, S., Chen, E., ... Ullrich, A. (1986). The complete primary structure of protein kinase C - The major phorbol ester receptor. Science, 233(4766), 853-859.

The complete primary structure of protein kinase C - The major phorbol ester receptor. / Parker, Peter J.; Coussens, Lisa; Totty, Nick; Rhee, Lucy; Young, Susan; Chen, Ellson; Stabel, Silvia; Waterfield, Michael D.; Ullrich, Axel.

In: Science, Vol. 233, No. 4766, 1986, p. 853-859.

Research output: Contribution to journalArticle

Parker, PJ, Coussens, L, Totty, N, Rhee, L, Young, S, Chen, E, Stabel, S, Waterfield, MD & Ullrich, A 1986, 'The complete primary structure of protein kinase C - The major phorbol ester receptor', Science, vol. 233, no. 4766, pp. 853-859.
Parker PJ, Coussens L, Totty N, Rhee L, Young S, Chen E et al. The complete primary structure of protein kinase C - The major phorbol ester receptor. Science. 1986;233(4766):853-859.
Parker, Peter J. ; Coussens, Lisa ; Totty, Nick ; Rhee, Lucy ; Young, Susan ; Chen, Ellson ; Stabel, Silvia ; Waterfield, Michael D. ; Ullrich, Axel. / The complete primary structure of protein kinase C - The major phorbol ester receptor. In: Science. 1986 ; Vol. 233, No. 4766. pp. 853-859.
@article{796498ddc2624ea1a4b2f6a1b1713054,
title = "The complete primary structure of protein kinase C - The major phorbol ester receptor",
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.",
author = "Parker, {Peter J.} and Lisa Coussens and Nick Totty and Lucy Rhee and Susan Young and Ellson Chen and Silvia Stabel and Waterfield, {Michael D.} and Axel Ullrich",
year = "1986",
language = "English (US)",
volume = "233",
pages = "853--859",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "4766",

}

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.

UR - http://www.scopus.com/inward/record.url?scp=0022545229&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0022545229&partnerID=8YFLogxK

M3 - Article

VL - 233

SP - 853

EP - 859

JO - Science

JF - Science

SN - 0036-8075

IS - 4766

ER -