Crystal structure of an ephrin ectodomain.
Crystal structure of an ephrin ectodomain.
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肝配蛋白胞外域的晶体结构。
DOI：
10.1016/s1534-5807(01)00002-8
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发表时间：
2001
期刊：
影响因子：
--
通讯作者：
Harrison,CJ
中科院分区：
文献类型：
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作者：
Toth,J;Cutforth,T;Gelinas,AD;Bethoney,KA;Bard,J;Harrison,CJ
Eph受体酪氨酸激酶和它们的膜相关配体肝配蛋白是轴突导向、细胞迁移、分裂和血管生成的重要调节因子。有两类脊椎动物肝配蛋白配体，它们对其同源受体具有不同的结合特异性。受体活化需要配体的多聚化，并且肝配蛋白配体本身在结合Eph受体时在细胞内发出信号。我们已经确定了小鼠ephrin-B2的胞外结构域的结构。肝配蛋白胞外域是一个八链β桶，与植物节瘤蛋白和植物蓝蛋白具有拓扑相似性。基于该结构，我们已经确定了Eph/肝配蛋白结合特异性和配体二聚化区域的潜在表面决定因素。肝配蛋白胞外域之间的高序列相似性表明，所有肝配蛋白可以模仿肝配蛋白-B2结构在这里提出。
Eph receptor tyrosine kinases and their membrane-associated ligands, the ephrins, are essential regulators of axon guidance, cell migration, segmentation, and angiogenesis. There are two classes of vertebrate ephrin ligands which have distinct binding specificities for their cognate receptors. Multimerization of the ligands is required for receptor activation, and ephrin ligands themselves signal intracellularly upon binding Eph receptors. We have determined the structure of the extracellular domain of mouse ephrin-B2. The ephrin ectodomain is an eight-stranded β barrel with topological similarity to plant nodulins and phytocyanins. Based on the structure, we have identified potential surface determinants of Eph/ephrin binding specificity and a ligand dimerization region. The high sequence similarity among ephrin ectodomains indicates that all ephrins may be modeled upon the ephrin-B2 structure presented here.