Title : An unusual cytokine:Ig-domain interaction revealed in the crystal
structure of leukemia inhibitory factor (
LIF ) in complex with the
LIF receptor
Abstract :
- Leukemia inhibitory factor (LIF) receptor is a cell surface receptor that mediates the actions of LIF and other IL-6 type cytokines through the formation of high-affinity signaling complexes with gp130
- Here we present the crystal structure of a complex of mouse LIF receptor with human LIF at 4.0 A resolution
- The structure is, to date, the largest cytokine receptor fragment determined by x-ray crystallography
- The binding of LIF to its receptor via the central Ig-like domain is unlike other cytokine receptor complexes that bind ligand predominantly through their cytokine-binding modules
- This structure, in combination with previous crystallographic studies, also provides a structural template to understand the formation and orientation of the high-affinity signaling complex between LIF , LIF receptor , and gp130