Small-Angle X-ray Scattering Study of Macrophage Migration Inhibitory Factor Complexed with Albumin |
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| Authors: | M. V. Petoukhov N. P. Gorbunov D. I. Svergun V. R. Samygina |
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| Affiliation: | 1.Shubnikov Institute of Crystallography of Federal Scientific Research Centre “Crystallography and Photonics,”,Russian Academy of Sciences,Moscow,Russia;2.European Molecular Biology Laboratory (EMBL),Hamburg,Germany;3.Frumkin Institute of Physical Chemistry and Electrochemistry,Russian Academy of Sciences,Moscow,Russia;4.Semenov Institute of Chemical Physics,Russian Academy of Sciences,Moscow,Russia;5.Institute for Experimental Medicine,St. Petersburg,Russia;6.Federal Research and Clinical Center of Physical-Chemical Medicine,Federal Medical Biological Agency,Moscow,Russia;7.St. Petersburg State University,St. Petersburg,Russia;8.Center of Preclinical and Translational Research, Almazov National Medical Research Center,Ministry of Health of the Russian Federation,St. Petersburg,Russia;9.National Research Centre “Kurchatov Institute,”,Moscow,Russia |
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| Abstract: | Macrophage migration inhibitory factor (MIF) is a proinflammatory cytokine, which plays a pivotal role in the regulation of immune response. Hence, the search for new inhibitors of MIF tautomerase activity has attracted great attention. This protein is known to serve as a superligand, by involving in protein–protein interactions that are poorly studied. Macrophage migration inhibitory factor was prepared in complex with albumin, and its solution structure was studied. Difficulties encountered in performing this research were due to the fact that the sample was a mixture of the MIF–albumin complex and the individual proteins. The interaction was found to be weak and unstable. Three most probable models of the MIF–albumin complex were obtained using small-angle X-ray scattering and molecular docking simulation, and one of these models was shown to be preferable. One albumin molecule binds to the MIF trimer in the active-site region of the protein. |
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