Goodall G J, Bagley C J, Vadas M A, Lopez A F
Hanson Centre for Cancer Research, Division of Human Immunology, Institute of Medical and Veterinary Science, Adelaide, South Australia.
Growth Factors. 1993;8(2):87-97. doi: 10.3109/08977199309046929.
The high affinity receptors for GM-CSF, IL-3 and IL-5 are heterodimers consisting of a ligand-specific alpha chain and a common beta chain. These proteins are members of a family of proteins known as the "cytokine receptor family" which is characterized by the presence of a 200-residue ligand-binding module. The GM-CSF, IL-3 and IL-5 receptor alpha chains constitute a distinct subgroup and share features not found in other members of the cytokine receptor family, features which we propose to be important for their interaction with the common beta chain and for their binding of the structurally-related ligands. The growth hormone receptor is a well-characterized member of the cytokine receptor family. Based on the structure of the complex between growth hormone and its receptor, we have proposed sites of contact between the GM-CSF, IL-3 and IL-5 receptors and their cognate ligands.
GM-CSF、IL-3和IL-5的高亲和力受体是异二聚体，由一个配体特异性α链和一个共同的β链组成。这些蛋白质是被称为“细胞因子受体家族”的蛋白质家族成员，其特征是存在一个200个残基的配体结合模块。GM-CSF、IL-3和IL-5受体α链构成一个独特的亚组，并具有细胞因子受体家族其他成员所没有的特征，我们认为这些特征对于它们与共同β链的相互作用以及与结构相关配体的结合很重要。生长激素受体是细胞因子受体家族中一个特征明确的成员。基于生长激素与其受体之间复合物的结构，我们提出了GM-CSF、IL-3和IL-5受体与其同源配体之间的接触位点。
