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.

authors

Huyton T,Zhang JG,Luo CS,Lou MZ,Hilton DJ,Nicola NA,Garrett TP

doi

10.1073/pnas.0705577104

subject

Has Abstract

pub_date

2007-07-31 00:00:00

pages

12737-42

issue

31

eissn

0027-8424

issn

1091-6490

pii

0705577104

journal_volume

104

pub_type

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