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.
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
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
Science
Date: Feb. 05, 1999
PubMed ID: 9933164
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