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Oligomeric structure of the human EphB2 receptor SAM domain.

Science (New York, N.Y.) | Feb 5, 1999

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 RIS Download

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