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

Jinzi J. Wu, Daniel E H Afar, Hoang Phan, Owen N. Witte, Kit Lam

Research output: Contribution to journalArticle

22 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)83-91
Number of pages9
JournalCombinatorial Chemistry and High Throughput Screening
Volume5
Issue number1
StatePublished - 2002

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Consensus Sequence
Protein-Tyrosine Kinases
Peptides
Proteins
Substrates
Cell signaling
Peptide Library
Phosphorylation
Protein-Serine-Threonine Kinases

ASJC Scopus subject areas

  • Chemistry (miscellaneous)
  • Clinical Biochemistry
  • Pharmacology

Cite this

Recognition of multiple substrate motifs by the c-ABL protein tyrosine kinase. / Wu, Jinzi J.; Afar, Daniel E H; Phan, Hoang; Witte, Owen N.; Lam, Kit.

In: Combinatorial Chemistry and High Throughput Screening, Vol. 5, No. 1, 2002, p. 83-91.

Research output: Contribution to journalArticle

Wu, Jinzi J. ; Afar, Daniel E H ; Phan, Hoang ; Witte, Owen N. ; Lam, Kit. / Recognition of multiple substrate motifs by the c-ABL protein tyrosine kinase. In: Combinatorial Chemistry and High Throughput Screening. 2002 ; Vol. 5, No. 1. pp. 83-91.
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