Результаты исследований: Материалы конференций › тезисы
Study of the interaction between mammalian MsrB1 and Trx proteins by NMR. / Yakimov, Alexander P.; Nerinovski, Kirill; Rychkov, Georgy; Shabalin, Konstantin; Dikiy, Alexander.
2011. 102 Реферат от Nuclear Magnetic Resonsnce Condense Matter, Санкт-Петербург, Российская Федерация.Результаты исследований: Материалы конференций › тезисы
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TY - CONF
T1 - Study of the interaction between mammalian MsrB1 and Trx proteins by NMR
AU - Yakimov, Alexander P.
AU - Nerinovski, Kirill
AU - Rychkov, Georgy
AU - Shabalin, Konstantin
AU - Dikiy, Alexander
PY - 2011/6/27
Y1 - 2011/6/27
N2 - Molecular oxygen is indispensable for survival of aerobic organisms, but the use of oxygen is also associated with the generation of reactive oxygen species (ROS).[1] ROS may damage various biomolecules such as DNA, proteins, and lipids, and may contribute to the development of cancer, neurodegenerative diseases and other maladies. This work is devoted to investigation of mammalian methionine sulfoxide reductase B1 (MsrB1) and thioredoxin (Trx) proteins constituting a part of defense system that protect cells against oxidative stress. MsrB1 protein utilizes catalytic redox-active cysteine/selenocystein residues to reverse oxidized methionine of damaged proteins back to reduced one.[2] Protein Trx is used to regenerate the active catalytic cystein/selenocystein of MsrB1. In this work we investigate mutant forms of proteins U95C MsrB1 and C35S Trx, which can organize stable but inactive protein complex. The aim of the work is to determine a possible spatial structure of these mutant proteins in complex.
AB - Molecular oxygen is indispensable for survival of aerobic organisms, but the use of oxygen is also associated with the generation of reactive oxygen species (ROS).[1] ROS may damage various biomolecules such as DNA, proteins, and lipids, and may contribute to the development of cancer, neurodegenerative diseases and other maladies. This work is devoted to investigation of mammalian methionine sulfoxide reductase B1 (MsrB1) and thioredoxin (Trx) proteins constituting a part of defense system that protect cells against oxidative stress. MsrB1 protein utilizes catalytic redox-active cysteine/selenocystein residues to reverse oxidized methionine of damaged proteins back to reduced one.[2] Protein Trx is used to regenerate the active catalytic cystein/selenocystein of MsrB1. In this work we investigate mutant forms of proteins U95C MsrB1 and C35S Trx, which can organize stable but inactive protein complex. The aim of the work is to determine a possible spatial structure of these mutant proteins in complex.
M3 - Abstract
SP - 102
Y2 - 27 June 2011 through 1 July 2011
ER -
ID: 74070081