By a News Reporter-Staff News Editor at Life Science Weekly -- A new study on Enzymes and Coenzymes is now available. According to news reporting originating in Moscow, Russia, by NewsRx journalists, research stated, "Copper-containing ferroxidase ceruloplasmin (Cp) forms binary and ternary complexes with cationic proteins lactoferrin (Lf) and myeloperoxidase (Mpo) during inflammation. We present an X-ray crystal structure of a 2Cp-Mpo complex at 4.7 A resolution."
The news reporters obtained a quote from the research from the Institute of Crystallography, "This structure allows one to identify major protein-protein interaction areas and provides an explanation for a competitive inhibition of Mpo by Cp and for the activation of p-phenylenediamine oxidation by Mpo. Small angle X-ray scattering was employed to construct low-resolution models of the Cp-Lf complex and, for the first time, of the ternary 2Cp-2Lf-Mpo complex in solution. The SAXS-based model of Cp-Lf supports the predicted 1:1 stoichiometry of the complex and demonstrates that both lobes of Lf contact domains 1 and 6 of Cp. The 2Cp-2Lf-Mpo SAXS model reveals the absence of interaction between Mpo and Lf in the ternary complex, so Cp can serve as a mediator of protein interactions in complex architecture. Mpo protects antioxidant properties of Cp by isolating its sensitive loop from proteases. The latter is important for incorporation of Fe(3+) into Lf, which activates ferroxidase activity of Cp and precludes oxidation of Cp substrates."
According to the news reporters, the research concluded: "Our models provide the structural basis for possible regulatory role of these complexes in preventing iron-induced oxidative damage."
For more information on this research see: Ceruloplasmin: macromolecular assemblies with iron-containing acute phase proteins. Plos One, 2013;8(7):e67145. (Public Library of Science - www.plos.org; Plos One - www.plosone.org)
Our news correspondents report that additional information may be obtained by contacting V.R. Samygina, Institute of Crystallography RAS, Moscow, Russia. Additional authors for this research include A.V. Sokolov, G. Bourenkov, M.V. Petoukhov, M.O. Pulina, E.T. Zakharova, V.B. Vasilyev, H. Bartunik and D.I Svergun (see also Enzymes and Coenzymes).
Keywords for this news article include: Moscow, Russia, Eurasia, Peptides, Amino Acids, Ceruloplasmin, Alphaglobulins, Blood Proteins, Nanotechnology, Metalloproteins, Oxidoreductases, Carrier Proteins, Acute Phase Proteins, Emerging Technologies, Enzymes and Coenzymes, Macromolecular Assemblies.
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