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

260 Scopus citations

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
JournalNature Methods
Volume1
Issue number1
DOIs
StatePublished - Oct 2004

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ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Hutti, J. E., Jarrell, E. T., Chang, J. D., Abbott, D. W., Storz, P., Toker, A., Cantley, L. C., & Turk, B. E. (2004). A rapid method for determining protein kinase phosphorylation specificity. Nature Methods, 1(1), 27-29. https://doi.org/10.1038/nmeth708