The signal transducer gp130: solution structure of the carboxy-terminal domain of the cytokine receptor homology region.
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.
Kernebeck
T
T
Institut für Biochemie, Rheinisch-Westfälische Technische Hochschule Aachen, Germany.
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
D000595:Amino Acid Sequence; D015703:Antigens, CD / Q000737:chemistry*; D050822:Cytokine Receptor gp130; D009682:Magnetic Resonance Spectroscopy; D008562:Membrane Glycoproteins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D018121:Receptors, Cytokine / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid
D015703:Antigens, CD; D008562:Membrane Glycoproteins; D018121:Receptors, Cytokine; D050822:Cytokine Receptor gp130