3tkr

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'''Unreleased structure'''
 
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The entry 3tkr is ON HOLD
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==Crystal structure of full-length human peroxiredoxin 4 with T118E mutation==
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<StructureSection load='3tkr' size='340' side='right'caption='[[3tkr]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3tkr]] is a 10 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=3TKR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TKR FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3tkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tkr OCA], [https://pdbe.org/3tkr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tkr RCSB], [https://www.ebi.ac.uk/pdbsum/3tkr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tkr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Prx4 (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.
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Authors: Wang, X., Wang, L., Wang, X., Sun, F., Wang, C.
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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<ref>PMID:21916849</ref>
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Description: Crystal structure of full-length human peroxiredoxin 4 with T118E mutation
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3tkr" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Peroxiredoxin 3D structures|Peroxiredoxin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Sun F]]
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[[Category: Wang C-C]]
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[[Category: Wang L]]
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[[Category: Wang X]]

Current revision

Crystal structure of full-length human peroxiredoxin 4 with T118E mutation

PDB ID 3tkr

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