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.
journal_name
Proc Natl Acad Sci U S Aauthors
Huyton T,Zhang JG,Luo CS,Lou MZ,Hilton DJ,Nicola NA,Garrett TPdoi
10.1073/pnas.0705577104subject
Has Abstractpub_date
2007-07-31 00:00:00pages
12737-42issue
31eissn
0027-8424issn
1091-6490pii
0705577104journal_volume
104pub_type
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