User:Cboursnell/Sandbox/Z/1-cysPrx C

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PDB 1xcc EBI.jpg
1-cys peroxidoxin from plasmodium yoelli
Symbol 1-cysPrx_C
Pfam PF10417
InterPro IPR019479

This entry represents the C-terminal domain of 1-Cys peroxiredoxin, a member of the peroxiredoxin superfamily which protect cells against membrane oxidation through glutathione (GSH)-dependent reduction of phospholipid hydroperoxides to corresponding alcohols.[1] The C-terminal domain is crucial for providing the extra cysteine necessary for dimerisation of the whole molecule. Loss of the enzyme's peroxidase activity is associated with oxidation of the catalytic cysteine found upstream of this domain. Glutathionylation, presumably through its disruption of protein structure, facilitates access for GSH, resulting in spontaneous reduction of the mixed disulphide to the sulphydryl and consequent activation of the enzyme.[2] The domain is associated with INTERPRO, which carries the catalytic cysteine.


  1. ^ Choi HJ, Kang SW, Yang CH, Rhee SG, Ryu SE (1998). "Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution". Nat. Struct. Biol. 5 (5): 400–6. PMID 9587003.  Unknown parameter |month= ignored (help); C1 control character in |pages= at position 5 (help)
  2. ^ Manevich Y, Feinstein SI, Fisher AB (2004). "Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST". Proc. Natl. Acad. Sci. U.S.A. 101 (11): 3780–5. doi:10.1073/pnas.0400181101. PMC 374321Freely accessible. PMID 15004285.  Unknown parameter |month= ignored (help); C1 control character in |pages= at position 6 (help)

This article incorporates text from the public domain Pfam and InterPro IPR019479

Category:Protein domains