Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

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