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| | <StructureSection load='3vww' size='340' side='right'caption='[[3vww]], [[Resolution|resolution]] 1.93Å' scene=''> | | <StructureSection load='3vww' size='340' side='right'caption='[[3vww]], [[Resolution|resolution]] 1.93Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3vww]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VWW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VWW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3vww]] is a 2 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=3VWW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VWW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.93Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2dml|2dml]], [[3vwu|3vwu]], [[3vwv|3vwv]], [[3w8j|3w8j]]</div></td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PDIA6, ERP5, P5, TXNDC7 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] </span></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=3vww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vww OCA], [https://pdbe.org/3vww PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vww RCSB], [https://www.ebi.ac.uk/pdbsum/3vww PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vww ProSAT]</span></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=3vww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vww OCA], [https://pdbe.org/3vww PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vww RCSB], [https://www.ebi.ac.uk/pdbsum/3vww PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vww ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PDIA6_HUMAN PDIA6_HUMAN]] May function as a chaperone that inhibits aggregation of misfolded proteins. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin.<ref>PMID:15466936</ref> <ref>PMID:12204115</ref>
| + | [https://www.uniprot.org/uniprot/PDIA6_HUMAN PDIA6_HUMAN] May function as a chaperone that inhibits aggregation of misfolded proteins. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin.<ref>PMID:15466936</ref> <ref>PMID:12204115</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Protein disulfide-isomerase]]
| + | [[Category: Inaba K]] |
| - | [[Category: Inaba, K]] | + | [[Category: Suzuki M]] |
| - | [[Category: Suzuki, M]] | + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Pdi family member]]
| + | |
| - | [[Category: Protein disulfide isomerase]]
| + | |
| - | [[Category: Thioredoxin fold]]
| + | |
| Structural highlights
Function
PDIA6_HUMAN May function as a chaperone that inhibits aggregation of misfolded proteins. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin.[1] [2]
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jordan PA, Stevens JM, Hubbard GP, Barrett NE, Sage T, Authi KS, Gibbins JM. A role for the thiol isomerase protein ERP5 in platelet function. Blood. 2005 Feb 15;105(4):1500-7. Epub 2004 Oct 5. PMID:15466936 doi:10.1182/blood-2004-02-0608
- ↑ Kikuchi M, Doi E, Tsujimoto I, Horibe T, Tsujimoto Y. Functional analysis of human P5, a protein disulfide isomerase homologue. J Biochem. 2002 Sep;132(3):451-5. PMID:12204115
- ↑ Sato Y, Kojima R, Okumura M, Hagiwara M, Masui S, Maegawa K, Saiki M, Horibe T, Suzuki M, Inaba K. Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding. Sci Rep. 2013 Aug 16;3:2456. doi: 10.1038/srep02456. PMID:23949117 doi:10.1038/srep02456
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