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Oligomeric structure of the human EphB2 receptor SAM domain.

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.

Pubmed ID: 9933164

Authors

  • Thanos CD
  • Goodwill KE
  • Bowie JU

Journal

Science (New York, N.Y.)

Publication Data

February 5, 1999

Associated Grants

None

Mesh Terms

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