Oligomeric structure of the human EphB2 receptor SAM domain

Science. 1999 Feb 5;283(5403):833-6. doi: 10.1126/science.283.5403.833.


The sterile alpha motif (SAM) domain is a protein interaction module that is present in diverse signal-transducing proteins. SAM domains are known to form homo- and hetero-oligomers. The crystal structure of the SAM domain from an Eph receptor tyrosine kinase, EphB2, reveals two large interfaces. In one interface, adjacent monomers exchange amino-terminal peptides that insert into a hydrophobic groove on each neighbor. A second interface is composed of the carboxyl-terminal helix and a nearby loop. A possible oligomer, constructed from a combination of these binding modes, may provide a platform for the formation of larger protein complexes.

Publication types

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

MeSH terms

  • Binding Sites
  • Crystallization
  • Crystallography, X-Ray
  • Dimerization
  • GRB10 Adaptor Protein
  • Humans
  • Hydrogen Bonding
  • Kinesins / metabolism
  • Models, Molecular
  • Myosins / metabolism
  • Phosphorylation
  • Protein Conformation*
  • Protein Structure, Secondary
  • Protein Tyrosine Phosphatases / metabolism
  • Proteins / metabolism
  • Receptor Aggregation
  • Receptor Protein-Tyrosine Kinases / chemistry*
  • Receptor Protein-Tyrosine Kinases / metabolism
  • Receptor, EphB2
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Surface Properties


  • AFDN protein, human
  • Proteins
  • Recombinant Proteins
  • GRB10 Adaptor Protein
  • Receptor Protein-Tyrosine Kinases
  • Receptor, EphB2
  • Protein Tyrosine Phosphatases
  • Myosins
  • Kinesins

Associated data

  • PDB/1B4F