Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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.
в: Biochemistry (Moscow), Том 83, № 6, 01.06.2018, стр. 701-707.Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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TY - JOUR
T1 - Structural Study of the Complex Formed by Ceruloplasmin and Macrophage Migration Inhibitory Factor
AU - Sokolov, A. V.
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.
PY - 2018/6/1
Y1 - 2018/6/1
N2 - 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.
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
KW - small-angle X-ray scattering
KW - X-ray analysis
UR - http://www.scopus.com/inward/record.url?scp=85048310374&partnerID=8YFLogxK
U2 - 10.1134/S000629791806007X
DO - 10.1134/S000629791806007X
M3 - Article
C2 - 30195326
AN - SCOPUS:85048310374
VL - 83
SP - 701
EP - 707
JO - Biochemistry (Moscow)
JF - Biochemistry (Moscow)
SN - 0006-2979
IS - 6
ER -
ID: 42247011