A rapid method for determining protein kinase phosphorylation specificity

Nat Methods. 2004 Oct;1(1):27-9. doi: 10.1038/nmeth708.

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.

Publication types

  • Evaluation Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Motifs
  • Binding Sites
  • Enzyme Activation
  • Microfluidic Analytical Techniques / methods*
  • Peptide Library*
  • Phosphorylation
  • Protein Binding
  • Protein Interaction Mapping / methods*
  • Protein-Serine-Threonine Kinases / analysis
  • Protein-Serine-Threonine Kinases / chemistry*
  • Protein-Serine-Threonine Kinases / metabolism*
  • Sequence Analysis, Protein / methods*
  • Substrate Specificity

Substances

  • Peptide Library
  • Protein-Serine-Threonine Kinases