PMID: 17652170

 

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Title : An unusual cytokine:Ig-domain interaction revealed in the crystal structure of leukemia inhibitory factor ( LIF ) in complex with the LIF receptor

Abstract :
  1. 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
  2. Here we present the crystal structure of a complex of mouse LIF receptor with human LIF at 4.0 A resolution
  3. The structure is, to date, the largest cytokine receptor fragment determined by x-ray crystallography
  4. 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
  5. 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