Kernebeck T, Pflanz S, Müller-Newen G, Kurapkat G, Scheek R M, Dijkstra K, Heinrich P C, Wollmer A, Grzesiek S, Grötzinger J
Institut für Biochemie, Rheinisch-Westfälische Technische Hochschule Aachen, Germany.
Protein Sci. 1999 Jan;8(1):5-12. doi: 10.1110/ps.8.1.5.
The transmembrane glycoprotein gp130 is the common signal transducing receptor subunit of the interleukin-6-type cytokines. It is a member of the cytokine-receptor superfamily predicted to consist of six domains in its extracellular part. The second and third domain constitute the cytokine-binding module defined by a set of four conserved cysteines and a WSXWS motif, respectively. The three-dimensional structure of the carboxy-terminal domain of this region was determined by multidimensional NMR. The domain consists of seven beta-strands constituting a fibronectin type III-like topology. The structure reveals that the WSDWS motif of gp130 is part of an extended tryptophan/arginine zipper which modulates the conformation of the CD loop.
跨膜糖蛋白gp130是白细胞介素-6型细胞因子的共同信号转导受体亚基。它是细胞因子受体超家族的成员,预计其细胞外部分由六个结构域组成。第二和第三结构域分别由一组四个保守的半胱氨酸和一个WSXWS基序构成细胞因子结合模块。该区域羧基末端结构域的三维结构通过多维核磁共振确定。该结构域由七条β链组成,构成类纤连蛋白III型拓扑结构。该结构表明,gp130的WSDWS基序是延伸的色氨酸/精氨酸拉链的一部分,可调节CD环的构象。