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Title: The crystal structure and biological function of leukemia inhibitory factor: implications for receptor binding
Authors: Robinson, R C ×
Grey, L M
Staunton, D
Vankelecom, Hugo
Vernallis, A B
Moreau, J F
Stuart, D I
Heath, J K
Jones, E Y #
Issue Date: Aug-1994
Series Title: Cell. vol:77 issue:7 pages:1101-16
Abstract: 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.
URI: 
ISSN: 0092-8674
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Laboratory of Tissue Plasticity (-)
× corresponding author
# (joint) last author

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