PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine

Science. 1995 May 26;268(5214):1177-9. doi: 10.1126/science.7539155.

Abstract

Src homology 2 (SH2) domains mediate assembly of signaling complexes by binding specifically to tyrosine-phosphorylated proteins. A phosphotyrosine binding (PTB) domain has been identified which also binds specifically to tyrosine-phosphorylated targets, but is structurally different from SH2 domains. Expression cloning was used to identify targets of PTB domains. PTB domains bound to phosphotyrosine within a sequence motif, asparagine-X1-X2-phosphotyrosine (where X represents any amino acid), that is found in many signaling proteins and is not recognized by SH2 domains. Mutational studies indicated that high affinity binding of PTB domains may require a specific conformation of the motif.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Binding Sites / physiology
  • Binding, Competitive
  • Cell Line
  • Humans
  • Molecular Sequence Data
  • Phosphopeptides / metabolism*
  • Phosphotyrosine
  • Protein Binding / physiology*
  • Recombinant Proteins / metabolism
  • Signal Transduction / physiology*
  • Tumor Cells, Cultured
  • Tyrosine / analogs & derivatives*
  • Tyrosine / metabolism

Substances

  • Phosphopeptides
  • Recombinant Proteins
  • Phosphotyrosine
  • Tyrosine