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Science 5 February 1999:
Vol. 283. no. 5403, pp. 833 - 836
DOI: 10.1126/science.283.5403.833
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Reports

Oligomeric Structure of the Human EphB2 Receptor SAM Domain

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

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.

UCLA-DOE Laboratory of Structural Biology and Molecular Medicine and Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095, USA.
*   To whom correspondence should be addressed. E-mail: bowie{at}mbi.ucla.edu

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Science. ISSN 0036-8075 (print), 1095-9203 (online)