Recognition of Multiple Substrate Motifs by the c-ABL Protein Tyrosine Kinase

Title: Recognition of Multiple Substrate Motifs by the c-ABL Protein Tyrosine Kinase

Volume: 5 Issue: 1

Author(s): Jinzi J. Wu, Daniel E.H. Afar, Hoang Phan, Owen N. Witte and Kit S. Lam

Affiliation:

Keywords: c-ABL Protein Tyrosine Kinase, serine threonine kinase stks, spodoptera frugiperda, peptide libraries

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.

Cite this article as:

Wu J. Jinzi, Afar E.H. Daniel, Phan Hoang, Witte N. Owen and Lam S. Kit, Recognition of Multiple Substrate Motifs by the c-ABL Protein Tyrosine Kinase, Combinatorial Chemistry & High Throughput Screening 2002; 5 (1) . https://dx.doi.org/10.2174/1386207023330516