Crystal structure of a cytokine-binding region of gp130

• Published in: The EMBO journal 1998-03, Vol.17 (6), p.1665-1674
• Main Authors: Bravo, Jerónimo, Staunton, David, Heath, John K., Jones, E.Yvonne
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Antigens, CD - chemistry; Binding Sites; Conserved Sequence - genetics; Crystallography, X-Ray; cytokine receptor; Cytokine Receptor gp130; Cytokines - metabolism; gp130; Humans; Ligands; Membrane Glycoproteins - chemistry; Models, Molecular; Molecular Sequence Data; multiple anomalous diffraction; Protein Conformation; Recombinant Fusion Proteins - chemistry; X-ray crystallography
• ISSN: 0261-4189; 1460-2075; 1460-2075
• DOI: 10.1093/emboj/17.6.1665

The structure of the cytokine‐binding homology region of the cell surface receptor gp130 has been determined by X‐ray crystallography at 2.0 Å resolution. The β 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°. 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.