Structure of the complete extracellular domain of the common β subunit of the human GM-CSF, IL-3, and IL-5 receptors reveals a novel dimer configuration
Structure of the complete extracellular domain of the common β subunit of the human GM-CSF, IL-3, and IL-5 receptors reveals a novel dimer configuration
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DOI：
10.1016/s0092-8674(01)00213-6
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发表时间：
2001-01-26
期刊：
影响因子：
64.5
通讯作者：
Young, IG
中科院分区：
文献类型：
--
作者：
Carr, PD;Gustin, SE;Young, IG
造血细胞因子GM-CSF、IL-3和IL-5的受体系统由配体特异性α受体亚基组成，其在共享β亚基（主要信号传导实体）的活化中起重要作用。在这里，我们报告完整的betac细胞外结构域的结构。它具有与迄今为止描述的任何I类细胞因子受体不同的结构，在不存在配体的情况下形成稳定的互锁二聚体，其中结构域1的G链氢键结合到二聚体相关分子的结构域3的相应β折叠中。结构域3的G链类似地与二聚体相关结构域1配对。该结构提供了新的见解受体激活各自的钌受体：配体复合物。
The receptor systems for the hemopoietic cytokines GM-CSF, IL-3, and IL-5 consist of ligand-specific alpha receptor subunits that play an essential role in the activation of the shared betac subunit, the major signaling entity. Here, we report the structure of the complete betac extracellular domain. It has a structure unlike any class I cytokine receptor described thus far, forming a stable interlocking dimer in the absence of ligand in which the G strand of domain 1 hydrogen bonds into the corresponding beta sheet of domain 3 of the dimer-related molecule. The G strand of domain 3 similarly partners with the dimer-related domain 1. The structure provides new insights into receptor activation by the respective ru receptor:ligand complexes.