3tkp: Difference between revisions
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==Crystal structure of full-length human peroxiredoxin 4 in the reduced form== | ==Crystal structure of full-length human peroxiredoxin 4 in the reduced form== | ||
<StructureSection load='3tkp' size='340' side='right' caption='[[3tkp]], [[Resolution|resolution]] 2.49Å' scene=''> | <StructureSection load='3tkp' size='340' side='right'caption='[[3tkp]], [[Resolution|resolution]] 2.49Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3tkp]] is a 5 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3tkp]] is a 5 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=3TKP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TKP FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.49Å</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=3tkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tkp OCA], [https://pdbe.org/3tkp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tkp RCSB], [https://www.ebi.ac.uk/pdbsum/3tkp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tkp ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 20: | Line 18: | ||
</div> | </div> | ||
<div class="pdbe-citations 3tkp" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3tkp" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Peroxiredoxin 3D structures|Peroxiredoxin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Sun | [[Category: Sun F]] | ||
[[Category: Wang | [[Category: Wang C-C]] | ||
[[Category: Wang | [[Category: Wang L]] | ||
[[Category: Wang | [[Category: Wang X]] | ||
Latest revision as of 20:33, 1 November 2023
Crystal structure of full-length human peroxiredoxin 4 in the reduced formCrystal structure of full-length human peroxiredoxin 4 in the reduced form
Structural highlights
FunctionPRDX4_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.[1] Publication Abstract from PubMedPrx4 (peroxiredoxin 4) is the only peroxiredoxin located in the ER (endoplasmic reticulum) and a proposed scavenger for H2O2. In this work we presented crystal structures of human Prx4 in three different redox forms and characterized the reaction features of Prx4 with H2O2. Prx4 exhibits a toroid-shaped decamer constructed of five catalytic dimers. Structural analysis revealed conformational changes around helix alpha2 and the C-terminal reigon with a YF motif from the partner subunit, which are required for inter-chain disulfide formation between Cys87 and Cys208, a critical step of the catalysis. The structural explanation for the restricting role of the YF motif on the active site dynamics is provided in detail. Prx4 has a high reactivity to H2O2, but is susceptible to over-oxidation and consequent inactivation by H2O2. Either deletion of the YF motif or dissociation into dimers decreased the susceptibility of Prx4 to over-oxidation by increasing the flexibility of Cys87. Structural insights into the peroxidase activity and inactivation of human peroxiredoxin 4.,Wang X, Wang L, Wang X, Sun F, Wang CC Biochem J. 2011 Sep 15. PMID:21916849[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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