1prx

<table><tr><td colspan='2'>[[1prx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PRX FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1prx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1prx OCA], [http://pdbe.org/1prx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1prx RCSB], [http://www.ebi.ac.uk/pdbsum/1prx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1prx ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/PRDX6_HUMAN PRDX6_HUMAN]] Involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury.

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Hydrogen peroxide (H2O2) has been implicated recently as an intracellular messenger that affects cellular processes including protein phosphorylation, transcription and apoptosis. A set of novel peroxidases, named peroxiredoxins (Prx), regulate the intracellular concentration of H2O2 by reducing it in the presence of an appropriate electron donor. The crystal structure of a human Prx enzyme, hORF6, reveals that the protein contains two discrete domains and forms a dimer. The N-terminal domain has a thioredoxin fold and the C-terminal domain is used for dimerization. The active site cysteine (Cys 47), which exists as cysteine-sulfenic acid in the crystal, is located at the bottom of a relatively narrow pocket. The positively charged environment surrounding Cys 47 accounts for the peroxidase activity of the enzyme, which contains no redox cofactors.

Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution.,Choi HJ, Kang SW, Yang CH, Rhee SG, Ryu SE Nat Struct Biol. 1998 May;5(5):400-6. PMID:9587003<ref>PMID:9587003</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1prx" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Human]]

[[Category: Choi, H J]]

[[Category: Kang, S W]]

[[Category: Rhee, S G]]

[[Category: Ryu, S E]]

[[Category: Yang, C H]]

[[Category: Redox regulation]]