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pubmed-article:17652170pubmed:abstractTextLeukemia 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.lld:pubmed
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pubmed-article:17652170pubmed:articleTitleAn unusual cytokine:Ig-domain interaction revealed in the crystal structure of leukemia inhibitory factor (LIF) in complex with the LIF receptor.lld:pubmed
pubmed-article:17652170pubmed:affiliationThe Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, Victoria 3050, Australia.lld:pubmed
pubmed-article:17652170pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:17652170pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
pubmed-article:17652170pubmed:publicationTypeResearch Support, N.I.H., Extramurallld:pubmed
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