Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase.

摘要: Abstract Background Src homology 2 (SH2) domains bind to phosphotyrosine residues in a sequence-specific manner, and thereby couple tyrosine phosphorylation changes the localization or catalytic activity of signal transducing molecules. Current understanding SH2 specificity is based on structures SH2–peptide complexes closely-related Lck kinases. The phosphatase Syp contains two that are relatively divergent from those kinases, with distinct target specificities, thus well suited for structural studies aimed at extending our specificity. Results Crystal amino-terminal domain separate high-affinity peptides, complex non-specific peptide uncomplexed form have been determined between 3 resolution. structure mode high- affinity binding essentially similar seen structures. However, interface more extensive Syp. Conclusions Most targets hydrophobic third position following phosphotyrosine, confirms anchored surface by this residue phosphotyrosine. In addition, has revealed sequence can extend across five shown how domain's topography be altered resulting specificity, while conserving central core domain.