2rii

From Proteopedia

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Template:STRUCTURE 2rii

Contents 1 Crystal Structure of Human Peroxiredoxin I in complex with Sulfiredoxin 2 Function 3 About this Structure 4 See Also 5 Reference

Crystal Structure of Human Peroxiredoxin I in complex with Sulfiredoxin

Template:ABSTRACT PUBMED 18172504

Function

[PRDX1_HUMAN] Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity). [SRXN1_HUMAN] Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4. Does not act on PRDX5 or PRDX6. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and a thioltransferase.^{[1] [2]}

About this Structure

2rii is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

• Peroxiredoxin

Reference

• Jonsson TJ, Johnson LC, Lowther WT. Structure of the sulphiredoxin-peroxiredoxin complex reveals an essential repair embrace. Nature. 2008 Jan 3;451(7174):98-101. PMID:18172504 doi:10.1038/nature06415

1. ↑ Chang TS, Jeong W, Woo HA, Lee SM, Park S, Rhee SG. Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine. J Biol Chem. 2004 Dec 3;279(49):50994-1001. Epub 2004 Sep 24. PMID:15448164 doi:10.1074/jbc.M409482200
2. ↑ Woo HA, Jeong W, Chang TS, Park KJ, Park SJ, Yang JS, Rhee SG. Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins. J Biol Chem. 2005 Feb 4;280(5):3125-8. Epub 2004 Dec 8. PMID:15590625 doi:10.1074/jbc.C400496200