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dc.contributor.authorDobrovolska, Olena
dc.contributor.authorRychkov, Georgy
dc.contributor.authorShumilina, Elena
dc.contributor.authorNerinovski, Kirill
dc.contributor.authorSchmidt, Alexander
dc.contributor.authorShabalin, Konstantin
dc.contributor.authorYakimov, Alexander
dc.contributor.authorDikiy, Alexander
dc.identifier.citationJournal of Biomedicine and Biotechnology. 2012, 2012 ID 586539-?.nb_NO
dc.description.abstractMaintenance of the cellular redox balance has vital importance for correcting organism functioning. Methionine sulfoxide reductases (Msrs) are among the key members of the cellular antioxidant defence system. To work properly, methionine sulfoxide reductases need to be reduced by their biological partner, thioredoxin (Trx). This process, according to the available kinetic data, represents the slowest step in the Msrs catalytic cycle. In the present paper, we investigated structural aspects of the intermolecular complex formation between mammalian MsrB1 and Trx. NMR spectroscopy and biocomputing were the two mostly used through the research approaches. The formation of NMR detectable MsrB1/Trx complex was monitored and studied in attempt to understand MsrB1 reduction mechanism. Using NMR data, molecular mechanics, protein docking, and molecular dynamics simulations, it was found that intermediate MsrB1/Trx complex is stabilized by interprotein β-layer. The complex formation accompanied by distortion of disulfide bond within MsrB1 facilitates the reduction of oxidized MsrB1 as it is evidenced by the obtained data.nb_NO
dc.publisherHindawi Publishing Corporationnb_NO
dc.rightsNavngivelse 4.0 Internasjonal*
dc.titleStructural Insights into Interaction between Mammalian Methionine Sulfoxide Reductase B1 and Thioredoxinnb_NO
dc.typeJournal articlenb_NO
dc.typePeer reviewednb_NO
dc.source.pagenumberID 586539-?nb_NO
dc.source.journalJournal of Biomedicine and Biotechnologynb_NO
dc.description.localcode© 2012 Olena Dobrovolska et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.nb_NO
cristin.unitnameInstitutt for bioteknologi og matvitenskap

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Navngivelse 4.0 Internasjonal
Except where otherwise noted, this item's license is described as Navngivelse 4.0 Internasjonal