Recognition of multiple substrate motifs by the c-ABL protein tyrosine kinase

Comb Chem High Throughput Screen. 2002 Feb;5(1):83-91. doi: 10.2174/1386207023330516.

Abstract

Using a combinatorial peptide library that is based on the one-bead one-peptide approach we identified 14 peptide substrates for the c-ABL protein tyrosine kinase, which define three distinct consensus sequence groups. This is distinct from many serine/threonine kinases, which often phosphorylate only one major consensus sequence. The three consensus sequences accurately predict phosphorylation sites in cellular ABL substrates proven to play a role in cell signaling. Our data suggest that protein tyrosine kinases have evolved to recognize multiple substrate motifs.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Motifs
  • Animals
  • Baculoviridae / genetics
  • Binding Sites
  • Consensus Sequence
  • Humans
  • Peptide Biosynthesis
  • Peptide Library
  • Peptides / isolation & purification
  • Proto-Oncogene Proteins c-abl / genetics
  • Proto-Oncogene Proteins c-abl / metabolism*
  • Spodoptera / genetics
  • Spodoptera / virology
  • Substrate Specificity

Substances

  • Peptide Library
  • Peptides
  • Proto-Oncogene Proteins c-abl