6FVE
Macrophage Migration Inhibitory Factor (MIF) with Covalently Bound FITC
Summary for 6FVE
| Entry DOI | 10.2210/pdb6fve/pdb |
| Descriptor | Macrophage migration inhibitory factor, 2-(6-hydroxy-3-oxo-3H-xanthen-9-yl)-5-[(E)-(sulfanylmethylidene)amino]benzoic acid, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | isomerase inhibitor, isomerase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 3 |
| Total formula weight | 38335.42 |
| Authors | Samygina, V.R.,Bourenkov, G.,Sokolov, A.V. (deposition date: 2018-03-02, release date: 2018-06-06, Last modification date: 2024-11-13) |
| Primary citation | 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. Biochemistry Mosc., 83:701-707, 2018 Cited by PubMed 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. PubMed: 30195326DOI: 10.1134/S000629791806007X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.41 Å) |
Structure validation
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