Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides

Nature. 1992 Aug 20;358(6388):646-53. doi: 10.1038/358646a0.

Abstract

Three-dimensional structures of complexes of the SH2 domain of the v-src oncogene product with two phosphotyrosyl peptides have been determined by X-ray crystallography at resolutions of 1.5 and 2.0 A, respectively. A central antiparallel beta-sheet in the structure is flanked by two alpha-helices, with peptide binding mediated by the sheet, intervening loops and one of the helices. The specific recognition of phosphotyrosine involves amino-aromatic interactions between lysine and arginine side chains and the ring system in addition to hydrogen-bonding interactions with the phosphate.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Crystallography
  • Macromolecular Substances
  • Models, Molecular
  • Molecular Sequence Data
  • Oncogene Protein pp60(v-src) / metabolism
  • Oncogene Protein pp60(v-src) / ultrastructure*
  • Peptides / metabolism
  • Phosphotyrosine
  • Protein Binding
  • Protein Conformation
  • Protein-Tyrosine Kinases / metabolism
  • Protein-Tyrosine Kinases / ultrastructure*
  • Sequence Alignment
  • Signal Transduction
  • Solvents
  • Tyrosine / analogs & derivatives*
  • Tyrosine / metabolism
  • X-Ray Diffraction

Substances

  • Macromolecular Substances
  • Peptides
  • Solvents
  • Phosphotyrosine
  • Tyrosine
  • Protein-Tyrosine Kinases
  • Oncogene Protein pp60(v-src)