Structure of the N-terminal SH3 domain of GRB2 complexed with a peptide from the guanine nucleotide releasing factor Sos

Nat Struct Biol. 1994 Dec;1(12):891-7. doi: 10.1038/nsb1294-891.


Src-homology 3 (SH3) domains mediate signal transduction by binding to proline-rich motifs in target proteins. We have determined the high-resolution NMR structure of the complex between the amino-terminal SH3 domain of GRB2 and a ten amino acid peptide derived from the guanine nucleotide releasing factor Sos. The NMR data show that the peptide adopts the conformation of a left-handed polyproline type II helix and interacts with three major sites on the SH3 domain. The orientation of the bound peptide is opposite to that of proline-rich peptides bound to the SH3 domains of Abl, Fyn and p85.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing*
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • GRB2 Adaptor Protein
  • Ligands
  • Magnetic Resonance Spectroscopy
  • Membrane Proteins / chemistry*
  • Membrane Proteins / genetics
  • Models, Molecular
  • Molecular Sequence Data
  • Molecular Structure
  • Peptide Fragments / chemistry
  • Peptide Fragments / genetics
  • Peptides / chemistry
  • Peptides / genetics
  • Proline-Rich Protein Domains
  • Protein Conformation
  • Protein Structure, Secondary
  • Proteins / chemistry*
  • Proteins / genetics
  • Sequence Homology, Amino Acid
  • Son of Sevenless Proteins


  • Adaptor Proteins, Signal Transducing
  • GRB2 Adaptor Protein
  • Ligands
  • Membrane Proteins
  • Peptide Fragments
  • Peptides
  • Proteins
  • Son of Sevenless Proteins