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  • Title: The signal transducer gp130: solution structure of the carboxy-terminal domain of the cytokine receptor homology region.
    Author: Kernebeck T, Pflanz S, Müller-Newen G, Kurapkat G, Scheek RM, Dijkstra K, Heinrich PC, Wollmer A, Grzesiek S, Grötzinger J.
    Journal: Protein Sci; 1999 Jan; 8(1):5-12. PubMed ID: 10210178.
    Abstract:
    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.
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