Structural Study of the Complex Formed by Ceruloplasmin and Macrophage Migration Inhibitory Factor

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

Research outputpeer-review

1 Citation (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)701-707
Number of pages7
JournalBiochemistry (Moscow)
Volume83
Issue number6
DOIs
Publication statusPublished - 1 Jun 2018

Scopus subject areas

  • Biochemistry

Cite this

Sokolov, A. V., Dadinova, L. A., Petoukhov, M. V., Bourenkov, G., Dubova, K. M., Amarantov, S. V., ... Samygina, V. R. (2018). Structural Study of the Complex Formed by Ceruloplasmin and Macrophage Migration Inhibitory Factor. Biochemistry (Moscow), 83(6), 701-707. https://doi.org/10.1134/S000629791806007X
Sokolov, A. V. ; Dadinova, L. A. ; Petoukhov, M. V. ; Bourenkov, G. ; Dubova, K. M. ; Amarantov, S. V. ; Volkov, V. V. ; Kostevich, V. A. ; Gorbunov, N. P. ; Grudinina, N. A. ; Vasilyev, V. B. ; Samygina, V. R. / Structural Study of the Complex Formed by Ceruloplasmin and Macrophage Migration Inhibitory Factor. In: Biochemistry (Moscow). 2018 ; Vol. 83, No. 6. pp. 701-707.
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Sokolov, AV, Dadinova, LA, Petoukhov, MV, Bourenkov, G, Dubova, KM, Amarantov, SV, Volkov, VV, Kostevich, VA, Gorbunov, NP, Grudinina, NA, Vasilyev, VB & Samygina, VR 2018, 'Structural Study of the Complex Formed by Ceruloplasmin and Macrophage Migration Inhibitory Factor', Biochemistry (Moscow), vol. 83, no. 6, pp. 701-707. https://doi.org/10.1134/S000629791806007X

Structural Study of the Complex Formed by Ceruloplasmin and Macrophage Migration Inhibitory Factor. / Sokolov, A. V.; Dadinova, L. A.; Petoukhov, M. V.; Bourenkov, G.; Dubova, K. M.; Amarantov, S. V.; Volkov, V. V.; Kostevich, V. A.; Gorbunov, N. P.; Grudinina, N. A.; Vasilyev, V. B.; Samygina, V. R.

In: Biochemistry (Moscow), Vol. 83, No. 6, 01.06.2018, p. 701-707.

Research outputpeer-review

TY - JOUR

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AU - Dadinova, L. A.

AU - Petoukhov, M. V.

AU - Bourenkov, G.

AU - Dubova, K. M.

AU - Amarantov, S. V.

AU - Volkov, V. V.

AU - Kostevich, V. A.

AU - Gorbunov, N. P.

AU - Grudinina, N. A.

AU - Vasilyev, V. B.

AU - Samygina, V. R.

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AB - 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.

KW - ceruloplasmin

KW - macrophage migration inhibitory factor

KW - protein–protein interactions

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