Huyton Trevor, Zhang Jian-Guo, Luo Cindy S, Lou Mei-Zhen, Hilton Douglas J, Nicola Nicos A, Garrett Thomas P J
The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, Victoria 3050, Australia.
Proc Natl Acad Sci U S A. 2007 Jul 31;104(31):12737-42. doi: 10.1073/pnas.0705577104. Epub 2007 Jul 24.
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.
白血病抑制因子（LIF）受体是一种细胞表面受体，它通过与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。在此，我们展示了小鼠LIF受体与人LIF复合物的晶体结构，分辨率为4.0埃。该结构是迄今为止通过X射线晶体学确定的最大的细胞因子受体片段。LIF通过中央免疫球蛋白样结构域与其受体结合，这与其他主要通过细胞因子结合模块结合配体的细胞因子受体复合物不同。该结构与先前的晶体学研究相结合，也为理解LIF、LIF受体和gp130之间高亲和力信号复合物的形成和取向提供了结构模板。
