Crystal structures of the human p56lck SH2 domain in complex with two short phosphotyrosyl peptides at 1.0 A and 1.8 A resolution.

@article{Tong1996CrystalSO,
  title={Crystal structures of the human p56lck SH2 domain in complex with two short phosphotyrosyl peptides at 1.0 A and 1.8 A resolution.},
  author={Liang Tong and Thomas C. Warren and Jonathan King and Raj Betageri and Jacky Ros{\'e} and Scott Jakes},
  journal={Journal of molecular biology},
  year={1996},
  volume={256 3},
  pages={601-10}
}
src homology 2 (SH2) domains are modules of about 100 amino acid residues and bind to phosphotyrosine-containing motifs in a sequence-specific manner. They play important roles in intracellular signal transduction and represent potential targets for pharmacological intervention. The protein tyrosine kinase p56lck is a member of the src family and is involved in T-cell activation. The crystal structure of its SH2 domain with an 11-residue peptide showed that the phosphotyrosine and the Ile… CONTINUE READING
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