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PDBsum entry 1lki
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References listed in PDB file
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Key reference
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Title
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The crystal structure and biological function of leukemia inhibitory factor: implications for receptor binding.
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Authors
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R.C.Robinson,
L.M.Grey,
D.Staunton,
H.Vankelecom,
A.B.Vernallis,
J.F.Moreau,
D.I.Stuart,
J.K.Heath,
E.Y.Jones.
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Ref.
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Cell, 1994,
77,
1101-1116.
[DOI no: ]
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PubMed id
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Abstract
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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.
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