View source for 3vwv


==crystal structure of N-terminally truncated peroxiredoxin 4 from M. musculus==
<StructureSection load='3vwv' size='340' side='right'caption='[[3vwv]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3vwv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VWV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VWV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vwv OCA], [https://pdbe.org/3vwv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vwv RCSB], [https://www.ebi.ac.uk/pdbsum/3vwv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vwv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PRDX4_MOUSE PRDX4_MOUSE] Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The mammalian endoplasmic reticulum (ER) harbors disulfide bond-generating enzymes, including Ero1alpha and peroxiredoxin 4 (Prx4), and nearly 20 members of the protein disulfide isomerase family (PDIs), which together constitute a suitable environment for oxidative protein folding. Here, we clarified the Prx4 preferential recognition of two PDI family proteins, P5 and ERp46, and the mode of interaction between Prx4 and P5 thioredoxin domain. Detailed analyses of oxidative folding catalyzed by the reconstituted Prx4-PDIs pathways demonstrated that, while P5 and ERp46 are dedicated to rapid, but promiscuous, disulfide introduction, PDI is an efficient proofreader of non-native disulfides. Remarkably, the Prx4-dependent formation of native disulfide bonds was accelerated when PDI was combined with ERp46 or P5, suggesting that PDIs work synergistically to increase the rate and fidelity of oxidative protein folding. Thus, the mammalian ER seems to contain highly systematized oxidative networks for the efficient production of large quantities of secretory proteins.

Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding.,Sato Y, Kojima R, Okumura M, Hagiwara M, Masui S, Maegawa K, Saiki M, Horibe T, Suzuki M, Inaba K Sci Rep. 2013 Aug 16;3:2456. doi: 10.1038/srep02456. PMID:23949117<ref>PMID:23949117</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3vwv" style="background-color:#fffaf0;"></div>

==See Also==
*[[Peroxiredoxin 3D structures|Peroxiredoxin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Inaba K]]
[[Category: Suzuki M]]