Crystal structure of a cytokine-binding region of gp130.
The structure of the cytokine-binding homology region of the cell surface receptor gp130 has been determined by X-ray crystallography at 2.0 A resolution. The beta sandwich structure of the two domains conforms to the topology of the cytokine receptor superfamily. This first structure of an uncomplexed receptor exhibits a similar L-shaped quaternary structure to that of ligand-bound family members and suggests a limited flexibility in relative domain orientation of some 3 degrees. The putative ligand-binding loops are relatively rigid, with a phenylalanine side chain similarly positioned to exposed aromatic residues implicated in ligand binding for other such receptors. The positioning and structure of the N-terminal portion of the polypeptide chain have implications for the structure and function of cytokine receptors, such as gp130, which contain an additional N-terminal immunoglobulin-like domain.
Bravo
J
J
Laboratory of Molecular Biophysics, The Rex Richards Building, South Parks Road, Oxford OX1 3QU.
Staunton
D
D
Heath
J K
JK
Jones
E Y
EY
D000595:Amino Acid Sequence; D015703:Antigens, CD / Q000737:chemistry*; D001665:Binding Sites; D017124:Conserved Sequence / Q000235:genetics; D018360:Crystallography, X-Ray; D050822:Cytokine Receptor gp130; D016207:Cytokines / Q000378:metabolism*; D006801:Humans; D008024:Ligands; D008562:Membrane Glycoproteins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins / Q000737:chemistry
D015703:Antigens, CD; D016207:Cytokines; C494199:IL6ST protein, human; D008024:Ligands; D008562:Membrane Glycoproteins; D011993:Recombinant Fusion Proteins; D050822:Cytokine Receptor gp130