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Oligomeric Structure of the Human EphB2 Receptor SAM Domain

1999; American Association for the Advancement of Science; Volume: 283; Issue: 5403 Linguagem: Inglês

10.1126/science.283.5403.833

1095-9203

Christopher D. Thanos, Kenneth E. Goodwill, James U. Bowie,

Ubiquitin and proteasome pathways

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.