• DOI:10.1016/S0960-9822(95)00060-1
Corpus ID: 16957239

Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases

@article{Mayer1995EvidenceTS,
  title={Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases},
  author={B. J. Mayer and H. Hirai and R. Sakai},
  journal={Current Biology},
  year={1995},
  volume={5},
  pages={296-305}
}

B. J. Mayer, H. Hirai, R. Sakai

Published 1995

Biology, Medicine

Current Biology

BACKGROUND Non-receptor protein-tyrosine kinases often contain at least one Src homology 2 (SH2) domain, a protein module that binds with high affinity to tyrosine-phosphorylated peptides. [...] Key Method We use chimeric mutants with heterologous SH2 domains to demonstrate that the SH2 domain of the oncogenically transforming adaptor protein Crk, which is the SH2 domain predicted to bind with highest affinity (of those tested) to potential phosphorylation sites in p130, is best able to facilitate…Expand Abstract

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