3hy2: Difference between revisions
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{{STRUCTURE_3hy2| PDB=3hy2 | SCENE= }} | {{STRUCTURE_3hy2| PDB=3hy2 | SCENE= }} | ||
===Crystal Structure of Sulfiredoxin in Complex with Peroxiredoxin I and ATP:Mg2+=== | ===Crystal Structure of Sulfiredoxin in Complex with Peroxiredoxin I and ATP:Mg2+=== | ||
{{ABSTRACT_PUBMED_19812042}} | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/PRDX1_HUMAN 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). [[http://www.uniprot.org/uniprot/SRXN1_HUMAN 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.<ref>PMID:15448164</ref> <ref>PMID:15590625</ref> | |||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID:019812042</ref><references group="xtra"/> | <ref group="xtra">PMID:019812042</ref><references group="xtra"/><references/> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Peroxiredoxin]] | [[Category: Peroxiredoxin]] | ||
Revision as of 05:37, 20 September 2013
Crystal Structure of Sulfiredoxin in Complex with Peroxiredoxin I and ATP:Mg2+Crystal Structure of Sulfiredoxin in Complex with Peroxiredoxin I and ATP:Mg2+
Template:ABSTRACT PUBMED 19812042
FunctionFunction
[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 StructureAbout this Structure
3hy2 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
- ↑ Jonsson TJ, Johnson LC, Lowther WT. Protein engineering of the quaternary sulfiredoxin.peroxiredoxin enzyme.substrate complex reveals the molecular basis for cysteine sulfinic acid phosphorylation. J Biol Chem. 2009 Nov 27;284(48):33305-10. Epub 2009 Oct 6. PMID:19812042 doi:10.1074/jbc.M109.036400
- ↑ 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
- ↑ 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