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==Crystal structure of a0-domain of P5 from H. sapiens== | |||
<StructureSection load='3vww' size='340' side='right' caption='[[3vww]], [[Resolution|resolution]] 1.93Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3vww]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VWW FirstGlance]. <br> | |||
==Function== | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2dml|2dml]], [[3vwu|3vwu]], [[3vwv|3vwv]], [[3w8j|3w8j]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PDIA6, ERP5, P5, TXNDC7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3vww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vww OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vww RCSB], [http://www.ebi.ac.uk/pdbsum/3vww PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://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> | [[http://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;"> | |||
== 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<ref>PMID:23949117</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein disulfide-isomerase]] | [[Category: Protein disulfide-isomerase]] | ||
[[Category: Inaba, K | [[Category: Inaba, K]] | ||
[[Category: Suzuki, M | [[Category: Suzuki, M]] | ||
[[Category: Isomerase]] | [[Category: Isomerase]] | ||
[[Category: Pdi family member]] | [[Category: Pdi family member]] | ||
[[Category: Protein disulfide isomerase]] | [[Category: Protein disulfide isomerase]] | ||
[[Category: Thioredoxin fold]] | [[Category: Thioredoxin fold]] | ||
Revision as of 01:07, 26 December 2014
Crystal structure of a0-domain of P5 from H. sapiensCrystal structure of a0-domain of P5 from H. sapiens
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 PubMedThe 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
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