An unusual cytokine: Ig-domain interaction revealed in the crystal structure of leukemia inhibitory factor (LIF) in complex with the LIF receptor
- Author(s)
- Huyton, T; Zhang, JG; Luo, CS; Lou, MZ; Hilton, DJ; Nicola, NA; Garrett, TPJ;
- Details
- Publication Year 2007-07-31,Volume 104,Issue #31,Page 12737-12742
- Journal Title
- PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Publication Type
- Journal Article
- 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 angstrom 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.
- Publisher
- NATL ACAD SCIENCES
- Keywords
- IMMUNOGLOBULIN-LIKE DOMAIN; EXTRACELLULAR DOMAINS; ALPHA-CHAIN; GP130; BINDING; AFFINITY; CELLS; RECOGNITION; ASSOCIATION; SUBUNITS
- Publisher's Version
- https://doi.org/10.1073/pnas.0705577104
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 2007-07-31 12:00:00