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

Citation
T. Kernebeck et al., The signal transducer gp130: Solution structure of the carboxy-terminal domain of the cytokine receptor homology region, PROTEIN SCI, 8(1), 1999, pp. 5-12
Citations number
46
Categorie Soggetti
Biochemistry & Biophysics
Journal title
PROTEIN SCIENCE
ISSN journal
09618368 → ACNP
Volume
8
Issue
1
Year of publication
1999
Pages
5 - 12
Database
ISI
SICI code
0961-8368(199901)8:1<5:TSTGSS>2.0.ZU;2-Y
Abstract
The transmembrane glycoprotein gp130 is the common signal transducing recep tor subunit of the interleukin-6-type cytokines. It is a member of the cyto kine-receptor superfamily predicted to consist of six domains in its extrac ellular part. The second and third domain constitute the cytokine-binding m odule defined by a set of four conserved cysteines and a WSXWS motif, respe ctively. 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 s tructure reveals that the WSDWS motif of gp130 is part of an extended trypt ophan/arginine zipper which modulates the conformation of the CD loop.