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. 2017 Jan 10;6(2):139–153. doi: 10.3892/mco.2017.1129

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Copyright: © Nicolussi et al.

This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.

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Figure 3. — Quaternary structure of PRDXs. (A) A-type dimers or B-type dimers. Certain components of the PRDX1 and PRDX6 subfamilies form a decameric structure through the interaction of five B-type dimers via the A-type dimer interface (A-type dimer colored in purple/blue; B-type dimer colored in blue/light blue). (B) The model of typical 2-Cys PRDX oligomerization and function: Different factors induce oligomerization of the dimers to hexa-, octa-, decamers or higher-order aggregates that are able to function as a peroxidase. Oxidation leads to the breakdown of the decamers, whereas hyperoxidation stabilizes the oligomer. Oxidized decamers can be reversed by sulfiredoxin (Srx) reduction (167). Hyperoxidized decamers are stable HMW complexes with chaperone-like activity. LMW, low molecular weight; HMW, high-molecular-weight; PRDX, peroxiredoxin.