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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >An unusual cytokine:lg-domain interaction revealed in the crystal structure of leukemia inhibitory factor (LIF) in complex with the LIF receptor
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An unusual cytokine:lg-domain interaction revealed in the crystal structure of leukemia inhibitory factor (LIF) in complex with the LIF receptor

机译：在与LIF受体复合的白血病抑制因子（LIF）的晶体结构中揭示了异常的细胞因子：Ig域相互作用

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摘要

Leukemia inhibitory factor (LIF) receptor is a cell surface receptor that mediates the actions of LIF and other IL-6 type cytokines through the formation of high-affinity signaling complexes with gp130. Here we present the crystal structure of a complex of mouse LIF receptor with human LIF at 4.0 A resolution. The structure is, to date, the largest cytokine receptor fragment determined by x-ray crystallography. The binding of LIF to its receptor via the central Ig-like domain is unlike other cytokine receptor complexes that bind ligand predominantly through their cytokine-binding modules. This structure, in combination with previous crystallographic studies, also provides a structural template to understand the formation and orientation of the high-affinity signaling complex between LIF, LIF receptor, and gp130.
机译：白血病抑制因子（LIF）受体是一种细胞表面受体，通过与gp130形成高亲和力信号复合物来介导LIF和其他IL-6型细胞因子的作用。在这里，我们介绍了小鼠LIF受体与人LIF在4.0 A分辨率下的复合物的晶体结构。迄今为止，该结构是通过X射线晶体学测定的最大的细胞因子受体片段。 LIF通过中央Ig样结构域与其受体的结合不同于其他主要通过其细胞因子结合模块结合配体的细胞因子受体复合物。该结构与先前的晶体学研究相结合，还提供了结构模板，以了解LIF，LIF受体和gp130之间的高亲和力信号复合物的形成和方向。

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