Triggering cell death: The crystal structure of Apo2L/TRAIL in a complex with death receptor 5
Triggering cell death: The crystal structure of Apo2L/TRAIL in a complex with death receptor 5
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DOI：
10.1016/s1097-2765(00)80207-5
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发表时间：
1999-10-01
期刊：
影响因子：
16
通讯作者：
de Vos, AM
中科院分区：
文献类型：
--
作者：
Hymowitz, SG;Christinger, HW;de Vos, AM
Apo 2L（也称为TRAIL）与其信号受体DR 4和DR 5之间的复合物的形成通过诱导细胞内死亡结构域的寡聚化来触发细胞凋亡。我们报告的晶体结构之间的复合物Apo 2L和DR 5的胞外域。该结构显示三个细长的受体依偎在同源三聚体配体的单体对之间的长缝隙中。界面分为两个不同的补丁，一个靠近受体细胞表面的复合物的底部附近，一个靠近顶部。两种贴片都含有对高亲和力结合至关重要的残基。比较的结构的α-光敏素受体复合物表明结合的一般原则和特异性的配体识别的TNF受体超家族。
Formation of a complex between Apo2L (also called TRAIL) and its signaling receptors, DR4 and DR5, triggers apoptosis by inducing the oligomerization of intracellular death domains. We report the crystal structure of the complex between Apo2L and the ectodomain of DR5. The structure shows three elongated receptors snuggled into long crevices between pairs of monomers of the homotrimeric ligand. The interface is divided into two distinct patches, one near the bottom of the complex close to the receptor cell surface and one near the top. Both patches contain residues that are critical for high-affinity binding. A comparison to the structure of the lymphotoxin-receptor complex suggests general principles of binding and specificity for ligand recognition in the TNF receptor superfamily.