Hexameric structure and assembly of the interleukin-6/IL-6 α-receptor/gp130 complex
Hexameric structure and assembly of the interleukin-6/IL-6 α-receptor/gp130 complex
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DOI：
10.1126/science.1083901
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发表时间：
2003-06-27
期刊：
影响因子：
56.9
通讯作者：
Garcia, KC
中科院分区：
文献类型：
--
作者：
Boulanger, MJ;Chow, DC;Garcia, KC
白细胞介素-6（IL-6）是一种免疫调节细胞因子，可激活由IL-6、IL-6 α-受体（IL-6 R α）和共享信号受体gp 130组成的细胞表面信号传导组件。细胞外信号传导复合物的3.65埃分辨率结构揭示了由总共10个与免疫相关的免疫偶联界面介导的六聚体互锁组装。六聚体复合物的组装顺序发生：IL-6是。rst被IL-6 R α接合，然后以适当的几何形状呈递给gp 130，以促进合作转变成高亲和力的、有信号传导能力的六聚体。其他IL-6/IL-12家族信号传导复合物的四级结构可能通过类似的拓扑蓝图构建。
Interleukin-6 (IL-6) is an immunoregulatory cytokine that activates a cell-surface signaling assembly composed of IL-6, the IL-6 alpha-receptor (IL-6Ralpha), and the shared signaling receptor gp130. The 3.65 angstrom - resolution structure of the extracellular signaling complex reveals a hexameric, interlocking assembly mediated by a total of 10 symmetry-related, thermodynamically coupled interfaces. Assembly of the hexameric complex occurs sequentially: IL-6 is. rst engaged by IL-6Ralpha and then presented to gp130 in the proper geometry to facilitate a cooperative transition into the high-affinity, signaling-competent hexamer. The quaternary structures of other IL-6/IL-12 family signaling complexes are likely constructed by means of a similar topological blueprint.