Oligomeric structure of the human EphB2 receptor SAM domain

被引:201
|
作者
Thanos, CD
Goodwill, KE
Bowie, JU [1 ]
机构
[1] Univ Calif Los Angeles, US DOE, Lab Struct Biol & Mol Med, Los Angeles, CA 90095 USA
[2] Univ Calif Los Angeles, Dept Chem, Los Angeles, CA 90095 USA
关键词
D O I
10.1126/science.283.5403.833
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
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页码:833 / 836
页数:4
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