Enviar artigo por via de e-mail Small-Angle X-ray Scattering Study of Macrophage Migration Inhibitory Factor Complexed with Albumin
- Autores: Petoukhov M.1,2,3,4, Sokolov A.5,6,7,8, Dadinova L.1, Gorbunov N.5, Svergun D.2, Samygina V.1,9
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Afiliações:
- Shubnikov Institute of Crystallography of Federal Scientific Research Centre “Crystallography and Photonics,”
- European Molecular Biology Laboratory (EMBL)
- Frumkin Institute of Physical Chemistry and Electrochemistry
- Semenov Institute of Chemical Physics
- Institute for Experimental Medicine
- Federal Research and Clinical Center of Physical-Chemical Medicine
- St. Petersburg State University
- Center of Preclinical and Translational Research, Almazov National Medical Research Center
- National Research Centre “Kurchatov Institute,”
- Edição: Volume 63, Nº 4 (2018)
- Páginas: 589-593
- Seção: Structure of Macromolecular Compounds
- URL: https://journals.rcsi.science/1063-7745/article/view/192689
- DOI: https://doi.org/10.1134/S106377451804020X
- ID: 192689
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Resumo
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.
Sobre autores
M. Petoukhov
Shubnikov Institute of Crystallography of Federal Scientific Research Centre “Crystallography and Photonics,”; European Molecular Biology Laboratory (EMBL); Frumkin Institute of Physical Chemistry and Electrochemistry; Semenov Institute of Chemical Physics
Email: lera@ns.crys.ras.ru
Rússia, Moscow, 119333; Hamburg, 22607; Moscow, 199071; Moscow, 117977
A. Sokolov
Institute for Experimental Medicine; Federal Research and Clinical Center of Physical-Chemical Medicine; St. Petersburg State University; Center of Preclinical and Translational Research, Almazov National Medical Research Center
Email: lera@ns.crys.ras.ru
Rússia, St. Petersburg, 197376; Moscow, 119435; St. Petersburg, 199034; St. Petersburg, 197341
L. Dadinova
Shubnikov Institute of Crystallography of Federal Scientific Research Centre “Crystallography and Photonics,”
Email: lera@ns.crys.ras.ru
Rússia, Moscow, 119333
N. Gorbunov
Institute for Experimental Medicine
Email: lera@ns.crys.ras.ru
Rússia, St. Petersburg, 197376
D. Svergun
European Molecular Biology Laboratory (EMBL)
Email: lera@ns.crys.ras.ru
Alemanha, Hamburg, 22607
V. Samygina
Shubnikov Institute of Crystallography of Federal Scientific Research Centre “Crystallography and Photonics,”; National Research Centre “Kurchatov Institute,”
Autor responsável pela correspondência
Email: lera@ns.crys.ras.ru
Rússia, Moscow, 119333; Moscow, 123098
