Biochemistry (Moscow) · 2018 · 10 citations · 9 references
Life SciencesBiochemistryMolecular BiologyEnzymologyProtein BiochemistryStructural BiologyEnzyme InhibitionMacromolecular StructureMacromolecular Structure DeterminationProtein Complex AnalysisProtein Complex AssemblyProtein StructureMacromolecular CrystallographyNoncompetitive InhibitionProtein Complex CharacterizationProtein Complex Structure DeterminationProtein CrystallographyProtein Structural AnalysisSmall-angle X-ray ScatteringStructural Characterization Of Complexes
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.
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Features and development of <i>Coot</i>
Paul Emsley, Bernhard Lohkamp, W. G. Scott et al. · Acta Crystallographica Section D Biological Crystallography · 2010 · 29.6K citations · Full text