Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
Structural insights into interaction between mammalian methionine sulfoxide reductase B1 and thioredoxin. / Dobrovolska, Olena; Rychkov, Georgy; Shumilina, Elena; Nerinovski, Kirill; Schmidt, Alexander; Shabalin, Konstantin; Yakimov, Alexander; Dikiy, Alexander.
в: Journal of Biomedicine and Biotechnology, Том 2012, 586539, 2012.Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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TY - JOUR
T1 - Structural insights into interaction between mammalian methionine sulfoxide reductase B1 and thioredoxin
AU - Dobrovolska, Olena
AU - Rychkov, Georgy
AU - Shumilina, Elena
AU - Nerinovski, Kirill
AU - Schmidt, Alexander
AU - Shabalin, Konstantin
AU - Yakimov, Alexander
AU - Dikiy, Alexander
N1 - Copyright: Copyright 2012 Elsevier B.V., All rights reserved.
PY - 2012
Y1 - 2012
N2 - Maintenance 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 -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.
AB - Maintenance 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 -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.
UR - http://www.scopus.com/inward/record.url?scp=84859726670&partnerID=8YFLogxK
U2 - 10.1155/2012/586539
DO - 10.1155/2012/586539
M3 - Article
C2 - 22505815
AN - SCOPUS:84859726670
VL - 2012
JO - BioMed Research International
JF - BioMed Research International
SN - 2314-6133
M1 - 586539
ER -
ID: 73950022