Publication Abstract from PubMed
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.
The signal transducer gp130: solution structure of the carboxy-terminal domain of the cytokine receptor homology region.,Kernebeck T, Pflanz S, Muller-Newen G, Kurapkat G, Scheek RM, Dijkstra K, Heinrich PC, Wollmer A, Grzesiek S, Grotzinger J Protein Sci. 1999 Jan;8(1):5-12. PMID:10210178[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
