3tkr
From Proteopedia
(Difference between revisions)
(6 intermediate revisions not shown.) | |||
Line 1: | Line 1: | ||
- | [[Image:3tkr.jpg|left|200px]] | ||
- | + | ==Crystal structure of full-length human peroxiredoxin 4 with T118E mutation== | |
- | + | <StructureSection load='3tkr' size='340' side='right'caption='[[3tkr]], [[Resolution|resolution]] 2.10Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <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> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</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=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> |
- | + | </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 == | ||
+ | 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. | ||
- | + | 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> | |
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 3tkr" style="background-color:#fffaf0;"></div> | ||
- | + | ==See Also== | |
- | + | *[[Peroxiredoxin 3D structures|Peroxiredoxin 3D structures]] | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | == | + | |
- | [[ | + | |
- | + | ||
- | == | + | |
- | < | + | |
[[Category: Homo sapiens]] | [[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]] |
- | + | ||
- | + | ||
- | + |
Current revision
Crystal structure of full-length human peroxiredoxin 4 with T118E mutation
|
Categories: Homo sapiens | Large Structures | Sun F | Wang C-C | Wang L | Wang X