Crystal structure of a cytokine-binding region of gp130.
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Bravo J, Staunton D, Heath JK, Jones EY
Crystal structure of a cytokine-binding region of gp130.
EMBO J. 1998 Mar 16;17(6):1665-74. doi: 10.1093/emboj/17.6.1665.
- PubMed ID
- 9501088 [ View in PubMed]
- 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.