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PDBsum entry 6fvh
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References listed in PDB file
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Key reference
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Title
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Structural study of the complex formed by ceruloplasmin and macrophage migration inhibitory factor.
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Authors
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A.V.Sokolov,
L.A.Dadinova,
M.V.Petoukhov,
G.Bourenkov,
K.M.Dubova,
S.V.Amarantov,
V.V.Volkov,
V.A.Kostevich,
N.P.Gorbunov,
N.A.Grudinina,
V.B.Vasilyev,
V.R.Samygina.
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Ref.
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Biochemistry (Mosc), 2018,
83,
701-707.
[DOI no: ]
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PubMed id
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Abstract
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Macrophage migration inhibitory factor (MIF) is a key proinflammatory cytokine.
Inhibitors of tautomerase activity of MIF are perspective antiinflammatory
compounds. Ceruloplasmin, the copper-containing ferroxidase of blood plasma, is
a noncompetitive inhibitor of tautomerase activity of MIF in the reaction with
p-hydroxyphenylpyruvate. Small-angle X-ray scattering established a model of the
complex formed by MIF and ceruloplasmin. Crystallographic analysis of MIF with a
modified active site supports the model. The stoichiometry of 3 CP/MIF trimer
complex was established using gel filtration. Conformity of novel data
concerning the interaction regions in the studied proteins with previous
biochemical data is discussed.
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