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

Authors: Wu J.J.; Afar D.E.H.; Phan H.; Witte O.N.; Lam K.S.

Source: Combinatorial Chemistry & High Throughput Screening, Volume 5, Number 1, February 2002 , pp. 83-91(10)

Publisher: Bentham Science Publishers

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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

Language: English

Document Type: Review article

DOI: 10.2174/1386207023330516

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