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.
Keywords: c-ABL Protein Tyrosine Kinase, serine threonine kinase stks, spodoptera frugiperda, peptide libraries
Combinatorial Chemistry & High Throughput Screening
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.
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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
DOI https://dx.doi.org/10.2174/1386207023330516 |
Print ISSN 1386-2073 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5402 |
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