Structural highlights
Function
[IL6RB_HUMAN] Signal-transducing molecule. The receptor systems for IL6, LIF, OSM, CNTF, IL11, CTF1 and BSF3 can utilize gp130 for initiating signal transmission. Binds to IL6/IL6R (alpha chain) complex, resulting in the formation of high-affinity IL6 binding sites, and transduces the signal. Does not bind IL6. May have a role in embryonic development (By similarity). The type I OSM receptor is capable of transducing OSM-specific signaling events.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
References
- ↑ Kernebeck T, Pflanz S, Muller-Newen G, Kurapkat G, Scheek RM, Dijkstra K, Heinrich PC, Wollmer A, Grzesiek S, Grotzinger J. The signal transducer gp130: solution structure of the carboxy-terminal domain of the cytokine receptor homology region. Protein Sci. 1999 Jan;8(1):5-12. PMID:10210178
