Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

The structure of murine leukemia inhibitory factor (LIF) has been determined by X-ray crystallography at 2.0 A resolution. The main chain fold conforms to the four alpha-helix bundle topology previously observed for several members of the hematopoietic cytokine family. Of these, LIF shows closest structural homology to granulocyte colony-stimulating factor and growth hormone (GH). Sequence alignments for the functionally related molecules oncostatin M and ciliary neurotrophic factor, when mapped to the LIF structure, indicate regions of conserved surface character. Analysis of the biological function and receptor specificity of a series of human-mouse LIF chimeras implicate two regions of receptor interaction that are located in the fourth helix and the preceding loop. A model for receptor binding based on the structure of the GH ligand-receptor complex requires additional, novel features to account for these data.


Journal article



Publication Date





1101 - 1116


Amino Acid Sequence, Animals, Crystallography, X-Ray, Growth Inhibitors, Interleukin-6, Leukemia Inhibitory Factor, Leukemia Inhibitory Factor Receptor alpha Subunit, Ligands, Lymphokines, Mice, Models, Molecular, Molecular Sequence Data, Protein Structure, Tertiary, Receptors, Cytokine, Receptors, OSM-LIF, Recombinant Fusion Proteins, Sequence Alignment, Sequence Homology, Amino Acid