The SH3 domain of Eps8 exists as a novel intertwined dimer

Nat Struct Biol. 1997 Sep;4(9):739-43. doi: 10.1038/nsb0997-739.


SH3 domains are structurally well-characterized as monomeric modular units of protein structure that mediate protein-protein recognition in numerous signal transduction proteins. The X-ray crystallographic structure of the Eps8 SH3 domain reveals a novel variation of the canonical SH3 fold: the SH3 domain from Eps8 is a dimer formed by strand interchange. In addition, co-immunoprecipitation experiments show that intact Eps8 is multimeric in vivo. Hence, the SH3 domain of Eps8 may represent a dimerization motif.

Publication types

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

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Amino Acid Sequence
  • Animals
  • COS Cells
  • Crystallography, X-Ray
  • Cytoskeletal Proteins
  • Dimerization
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Precipitin Tests
  • Protein Conformation
  • Proteins / chemistry*
  • Proteins / genetics
  • Recombinant Fusion Proteins
  • Sequence Alignment
  • src Homology Domains*


  • Adaptor Proteins, Signal Transducing
  • Cytoskeletal Proteins
  • Eps8 protein, mouse
  • Proteins
  • Recombinant Fusion Proteins