2Q7N

Crystal structure of Leukemia inhibitory factor in complex with LIF receptor (domains 1-5)

Summary for 2Q7N

• Entry DOI: 10.2210/pdb2q7n/pdb
• Related: 1PVH
• Descriptor: Leukemia inhibitory factor receptor, Leukemia inhibitory factor, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• Functional Keywords: cytokine cell surface receptor complex lifr lif, cytokine receptor-cytokine complex, cytokine receptor/cytokine
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 4
• Total formula weight: 158379.13

Authors

Huyton, T.,Zhang, J.G.,Nicola, N.A.,Garrett, T.P.J. (deposition date: 2007-06-07, release date: 2007-07-31, Last modification date: 2024-11-06)

Primary citation

Huyton, T.,Zhang, J.G.,Luo, C.S.,Lou, M.Z.,Hilton, D.J.,Nicola, N.A.,Garrett, T.P.
An unusual cytokine:Ig-domain interaction revealed in the crystal structure of leukemia inhibitory factor (LIF) in complex with the LIF receptor.
Proc.Natl.Acad.Sci.USA, 104:12737-12742, 2007

PubMed 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.

PubMed: 17652170
DOI: 10.1073/pnas.0705577104

Experimental method

X-RAY DIFFRACTION (4 Å)