| Literature DB >> 10210178 |
T Kernebeck1, S Pflanz, G Müller-Newen, G Kurapkat, R M Scheek, K Dijkstra, P C Heinrich, A Wollmer, S Grzesiek, J Grötzinger.
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.Entities:
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Year: 1999 PMID: 10210178 PMCID: PMC2144119 DOI: 10.1110/ps.8.1.5
Source DB: PubMed Journal: Protein Sci ISSN: 0961-8368 Impact factor: 6.725