Crystal structure of a cytokine-binding region of gp130.

Journal article

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.

Authors: Bravo, J; Staunton, D; Heath, J; Jones, E

• Publication status: Published
• Journal: EMBO journal
• Volume: 17
• Issue: 6
• Pages: 1665-1674
• Publication date: 1998-03-01
• DOI: 10.1093/emboj/17.6.1665
• EISSN: 1460-2075
• ISSN: 0261-4189
• Language: English
• Keywords: Recombinant Fusion Proteins; Membrane Glycoproteins; Binding Sites; Conserved Sequence; Molecular Sequence Data; Crystallography, X-Ray; Cytokines; Antigens, CD; Protein Conformation; Amino Acid Sequence; Cytokine Receptor gp130; Ligands; Models, Molecular; Humans