Macromolecular Crystallography Laboratory, NCI-Frederick, Frederick, MD 21702, USA.
J Mol Biol. 2010 Dec 10;404(4):650-64. doi: 10.1016/j.jmb.2010.09.068. Epub 2010 Oct 8.
Interferon (IFN)-λ1 [also known as interleukin (IL)-29] belongs to the recently discovered group of type III IFNs. All type III IFNs initiate signaling processes through formation of specific heterodimeric receptor complexes consisting of IFN-λR1 and IL-10R2. We have determined the structure of human IFN-λ1 complexed with human IFN-λR1, a receptor unique to type III IFNs. The overall structure of IFN-λ1 is topologically similar to the structure of IL-10 and other members of the IL-10 family of cytokines. IFN-λR1 consists of two distinct domains having fibronectin type III topology. The ligand-receptor interface includes helix A, loop AB, and helix F on the IFN site, as well as loops primarily from the N-terminal domain and inter-domain hinge region of IFN-λR1. Composition and architecture of the interface that includes only a few direct hydrogen bonds support an idea that long-range ionic interactions between ligand and receptor govern the process of initial recognition of the molecules while hydrophobic interactions finalize it.
干扰素（IFN）-λ1[也称为白细胞介素（IL）-29]属于最近发现的 III 型 IFN 家族。所有 III 型 IFN 通过形成由 IFN-λR1 和 IL-10R2 组成的特定异二聚体受体复合物来启动信号转导过程。我们已经确定了与人 IFN-λR1 结合的人 IFN-λ1 的结构，IFN-λR1 是 III 型 IFN 特有的受体。IFN-λ1 的整体结构在拓扑上与 IL-10 和细胞因子 IL-10 家族的其他成员的结构相似。IFN-λR1 由具有纤维连接蛋白 III 拓扑结构的两个不同结构域组成。配体-受体界面包括 IFN 上的 A 螺旋、AB 环和 F 螺旋，以及主要来自 IFN-λR1 的 N 端结构域和结构域间铰链区的环。仅包含少数直接氢键的界面组成支持这样一种观点，即配体和受体之间的长程离子相互作用控制分子初始识别的过程，而疏水性相互作用则使其最终确定。
