Oligomeric structure of the human EphB2 receptor SAM domain
Oligomeric structure of the human EphB2 receptor SAM domain
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DOI：
10.1126/science.283.5403.833
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发表时间：
1999-02-05
期刊：
影响因子：
56.9
通讯作者：
Bowie, JU
中科院分区：
文献类型：
--
作者：
Thanos, CD;Goodwill, KE;Bowie, JU
无菌α基序（SAM）结构域是存在于多种信号转导蛋白中的蛋白质相互作用模块。已知SAM结构域形成同源寡聚体和异源寡聚体。来自Eph受体酪氨酸激酶EphB2的SAM结构域的晶体结构揭示了两个大界面。在一个界面中，相邻的单体交换氨基末端肽，这些肽插入每个相邻单体上的疏水沟中。第二个界面由羧基末端螺旋和附近的Loop组成。由这些结合模式的组合构建的可能的寡聚体可以为形成更大的蛋白质复合物提供平台。
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.