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

  • THOMAS KERNEBECK (a1), STEFAN PFLANZ (a1), GERHARD MÜLLER-NEWEN (a1), GÜNTHER KURAPKAT (a1), RUUD M. SCHEEK (a2), KLAAS DIJKSTRA (a2), PETER C. HEINRICH (a1), AXEL WOLLMER (a1), STEPHAN GRZESIEK (a3) and JOACHIM GRÖTZINGER (a1)...

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 β-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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Corresponding author

Reprint requests to: J. Grötzinger, Institut für Biochemie, RWTH-Aachen, Pauwelsstraße 30, D-52057 Aachen, Germany; e-mail: achim@bionm1.biochem.rwth-aachen.de.

Keywords

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

  • THOMAS KERNEBECK (a1), STEFAN PFLANZ (a1), GERHARD MÜLLER-NEWEN (a1), GÜNTHER KURAPKAT (a1), RUUD M. SCHEEK (a2), KLAAS DIJKSTRA (a2), PETER C. HEINRICH (a1), AXEL WOLLMER (a1), STEPHAN GRZESIEK (a3) and JOACHIM GRÖTZINGER (a1)...

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