View source for 5hqp


==Crystal structure of the ERp44-peroxiredoxin 4 complex==
<StructureSection load='5hqp' size='340' side='right'caption='[[5hqp]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5hqp]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HQP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HQP 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]] 2.6&#8491;</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=5hqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hqp OCA], [https://pdbe.org/5hqp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hqp RCSB], [https://www.ebi.ac.uk/pdbsum/5hqp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hqp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PRDX4_HUMAN PRDX4_HUMAN] 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.<ref>PMID:9388242</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
ERp44 controls the localization and transport of diverse proteins in the early secretory pathway. The mechanisms that allow client recognition and the source of the oxidative power for forming intermolecular disulfides are as yet unknown. Here we present the structure of ERp44 bound to a client, peroxiredoxin 4. Our data reveal that ERp44 binds the oxidized form of peroxiredoxin 4 via thiol-disulfide interchange reactions. The structure explains the redox-dependent recognition and characterizes the essential non-covalent interactions at the interface. The ERp44-Prx4 covalent complexes can be reduced by glutathione and protein disulfide isomerase family members in the ER, allowing the two components to recycle. This work provides insights into the mechanisms of thiol-mediated protein retention and indicates the key roles of ERp44 in this biochemical cycle to optimize oxidative folding and redox homeostasis.

Crystal Structure of the ERp44-Peroxiredoxin 4 Complex Reveals the Molecular Mechanisms of Thiol-Mediated Protein Retention.,Yang K, Li DF, Wang X, Liang J, Sitia R, Wang CC, Wang X Structure. 2016 Oct 4;24(10):1755-1765. doi: 10.1016/j.str.2016.08.002. Epub 2016, Sep 15. PMID:27642162<ref>PMID:27642162</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5hqp" style="background-color:#fffaf0;"></div>

==See Also==
*[[Peroxiredoxin 3D structures|Peroxiredoxin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Li DF]]
[[Category: Wang CC]]
[[Category: Wang X]]
[[Category: Yang K]]