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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Robinson, R.C. et al.

The crystal structure and biological function of leukemia inhibitory factor: implications for receptor binding.

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.[1]

References

The crystal structure and biological function of leukemia inhibitory factor: implications for receptor binding. Robinson, R.C., Grey, L.M., Staunton, D., Vankelecom, H., Vernallis, A.B., Moreau, J.F., Stuart, D.I., Heath, J.K., Jones, E.Y. Cell (1994) [Pubmed]

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