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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.

Original publication

DOI

10.1093/emboj/17.6.1665

Type

Journal article

Journal

EMBO J

Publication Date

16/03/1998

Volume

17

Pages

1665 - 1674

Keywords

Amino Acid Sequence, Antigens, CD, Binding Sites, Conserved Sequence, Crystallography, X-Ray, Cytokine Receptor gp130, Cytokines, Humans, Ligands, Membrane Glycoproteins, Models, Molecular, Molecular Sequence Data, Protein Conformation, Recombinant Fusion Proteins