We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Crystal structure of a cytokine-binding region of gp130.
- Authors
Bravo, J; Staunton, D; Heath, J K; Jones, E Y
- Abstract
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.
- Publication
The EMBO journal, 1998, Vol 17, Issue 6, p1665
- ISSN
0261-4189
- Publication type
Journal Article
- DOI
10.1093/emboj/17.6.1665