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

Kernebeck, T. and Pflanz, S. and Muller-Newen, G. and Kurapkat, G. and Scheek, R. M. and Dijkstra, K. and Heinrich, P. C. and Wollmer, A. and Grzesiek, S. and Grotzinger, J.. (1999) The signal transducer gp130 : solution structure of the carboxy-terminal domain of the cytokine receptor homology region. Protein Science, 8 (1). pp. 5-12.

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Official URL: http://edoc.unibas.ch/dok/A5258813

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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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Grzesiek)
UniBasel Contributors:Grzesiek, Stephan
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Cambridge University Press
ISSN:0961-8368
e-ISSN:1469-896X
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:23 Nov 2017 15:15
Deposited On:22 Mar 2012 13:21

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