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The signal transducer gp130: solution structure of the carboxy-terminal domain of the cytokine receptor homology region.

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.

SUBMITTER: Kernebeck T

PROVIDER: S-EPMC2144119 | biostudies-other | 1999 Jan

REPOSITORIES: biostudies-other

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The signal transducer gp130: solution structure of the carboxy-terminal domain of the cytokine receptor homology region.

Kernebeck T T Pflanz S S Müller-Newen G G Kurapkat G G Scheek R M RM Dijkstra K K Heinrich P C PC Wollmer A A Grzesiek S S Grötzinger J J

Protein science : a publication of the Protein Society 19990101 1

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 ...[more]

PMID: 10210178

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