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Combinatorial Chemistry & High Throughput Screening

Editor-in-Chief

ISSN (Print): 1386-2073
ISSN (Online): 1875-5402

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

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

Volume 5, Issue 1, 2002

Page: [83 - 91] Pages: 9

DOI: 10.2174/1386207023330516

Price: $65

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


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