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) |
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UniBasel Contributors: | Grzesiek, Stephan |
Item Type: | Article, refereed |
Article Subtype: | Research Article |
Publisher: | Cambridge University Press |
ISSN: | 0961-8368 |
e-ISSN: | 1469-896X |
Note: | Publication type according to Uni Basel Research Database: Journal article |
Identification Number: |
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Last Modified: | 23 Nov 2017 15:15 |
Deposited On: | 22 Mar 2012 13:21 |
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