A rapid method for determining protein kinase phosphorylation specificity.

Jessica E. Hutti, Emily T. Jarrell, James D. Chang, Derek W. Abbott, Peter Storz, Alex Toker, Lewis C. Cantley, Benjamin E. Turk

Research output: Contribution to journalArticle

254 Citations (Scopus)

Abstract

Selection of target substrates by protein kinases is strongly influenced by the amino acid sequence surrounding the phosphoacceptor site. Identification of the preferred peptide phosphorylation motif for a given kinase permits the production of efficient peptide substrates and greatly simplifies the mapping of phosphorylation sites in protein substrates. Here we describe a combinatorial peptide library method that allows rapid generation of phosphorylation motifs for serine/threonine kinases.

Original languageEnglish (US)
Pages (from-to)27-29
Number of pages3
JournalNat Methods
Volume1
Issue number1
StatePublished - Oct 2004
Externally publishedYes

Fingerprint

Phosphorylation
Protein Kinases
Substrates
Peptide Library
Peptides
Protein-Serine-Threonine Kinases
Amino Acid Sequence
Phosphotransferases
Amino Acids
Proteins

ASJC Scopus subject areas

  • Biotechnology
  • Molecular Biology
  • Cell Biology

Cite this

Hutti, J. E., Jarrell, E. T., Chang, J. D., Abbott, D. W., Storz, P., Toker, A., ... Turk, B. E. (2004). A rapid method for determining protein kinase phosphorylation specificity. Nat Methods, 1(1), 27-29.

A rapid method for determining protein kinase phosphorylation specificity. / Hutti, Jessica E.; Jarrell, Emily T.; Chang, James D.; Abbott, Derek W.; Storz, Peter; Toker, Alex; Cantley, Lewis C.; Turk, Benjamin E.

In: Nat Methods, Vol. 1, No. 1, 10.2004, p. 27-29.

Research output: Contribution to journalArticle

Hutti, JE, Jarrell, ET, Chang, JD, Abbott, DW, Storz, P, Toker, A, Cantley, LC & Turk, BE 2004, 'A rapid method for determining protein kinase phosphorylation specificity.', Nat Methods, vol. 1, no. 1, pp. 27-29.
Hutti JE, Jarrell ET, Chang JD, Abbott DW, Storz P, Toker A et al. A rapid method for determining protein kinase phosphorylation specificity. Nat Methods. 2004 Oct;1(1):27-29.
Hutti, Jessica E. ; Jarrell, Emily T. ; Chang, James D. ; Abbott, Derek W. ; Storz, Peter ; Toker, Alex ; Cantley, Lewis C. ; Turk, Benjamin E. / A rapid method for determining protein kinase phosphorylation specificity. In: Nat Methods. 2004 ; Vol. 1, No. 1. pp. 27-29.
@article{f3c3af5c5bbf4aa0ad7fdef7b52e849e,
title = "A rapid method for determining protein kinase phosphorylation specificity.",
abstract = "Selection of target substrates by protein kinases is strongly influenced by the amino acid sequence surrounding the phosphoacceptor site. Identification of the preferred peptide phosphorylation motif for a given kinase permits the production of efficient peptide substrates and greatly simplifies the mapping of phosphorylation sites in protein substrates. Here we describe a combinatorial peptide library method that allows rapid generation of phosphorylation motifs for serine/threonine kinases.",
author = "Hutti, {Jessica E.} and Jarrell, {Emily T.} and Chang, {James D.} and Abbott, {Derek W.} and Peter Storz and Alex Toker and Cantley, {Lewis C.} and Turk, {Benjamin E.}",
year = "2004",
month = "10",
language = "English (US)",
volume = "1",
pages = "27--29",
journal = "PLoS Medicine",
issn = "1549-1277",
publisher = "Nature Publishing Group",
number = "1",

}

TY - JOUR

T1 - A rapid method for determining protein kinase phosphorylation specificity.

AU - Hutti, Jessica E.

AU - Jarrell, Emily T.

AU - Chang, James D.

AU - Abbott, Derek W.

AU - Storz, Peter

AU - Toker, Alex

AU - Cantley, Lewis C.

AU - Turk, Benjamin E.

PY - 2004/10

Y1 - 2004/10

N2 - Selection of target substrates by protein kinases is strongly influenced by the amino acid sequence surrounding the phosphoacceptor site. Identification of the preferred peptide phosphorylation motif for a given kinase permits the production of efficient peptide substrates and greatly simplifies the mapping of phosphorylation sites in protein substrates. Here we describe a combinatorial peptide library method that allows rapid generation of phosphorylation motifs for serine/threonine kinases.

AB - Selection of target substrates by protein kinases is strongly influenced by the amino acid sequence surrounding the phosphoacceptor site. Identification of the preferred peptide phosphorylation motif for a given kinase permits the production of efficient peptide substrates and greatly simplifies the mapping of phosphorylation sites in protein substrates. Here we describe a combinatorial peptide library method that allows rapid generation of phosphorylation motifs for serine/threonine kinases.

UR - http://www.scopus.com/inward/record.url?scp=17644391197&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=17644391197&partnerID=8YFLogxK

M3 - Article

C2 - 15782149

AN - SCOPUS:17644391197

VL - 1

SP - 27

EP - 29

JO - PLoS Medicine

JF - PLoS Medicine

SN - 1549-1277

IS - 1

ER -