3uj1: Difference between revisions
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==Crystal structure of the third thioredoxin domain of human ERp46== | ==Crystal structure of the third thioredoxin domain of human ERp46== | ||
<StructureSection load='3uj1' size='340' side='right' caption='[[3uj1]], [[Resolution|resolution]] 2.65Å' scene=''> | <StructureSection load='3uj1' size='340' side='right'caption='[[3uj1]], [[Resolution|resolution]] 2.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3uj1]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3uj1]] is a 1 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=3UJ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UJ1 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]] 2.651Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3uj1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uj1 OCA], [https://pdbe.org/3uj1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uj1 RCSB], [https://www.ebi.ac.uk/pdbsum/3uj1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uj1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/TXND5_HUMAN TXND5_HUMAN] Possesses thioredoxin activity. Has been shown to reduce insulin disulfide bonds. Also complements protein disulfide-isomerase deficiency in yeast (By similarity). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3uj1" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Ferrari DM]] | ||
[[Category: | [[Category: Funkner A]] | ||
[[Category: | [[Category: Parthier C]] | ||
[[Category: | [[Category: Stubbs MT]] | ||
Latest revision as of 13:32, 6 November 2024
Crystal structure of the third thioredoxin domain of human ERp46Crystal structure of the third thioredoxin domain of human ERp46
Structural highlights
FunctionTXND5_HUMAN Possesses thioredoxin activity. Has been shown to reduce insulin disulfide bonds. Also complements protein disulfide-isomerase deficiency in yeast (By similarity). Publication Abstract from PubMedThe protein disulfide isomerase (PDI) family member ERp46/endoPDI/thioredoxin domain-containing protein 5 is preferentially expressed in a limited number of tissues, where it may function as a survival factor for nitrosative stress in vivo. It is involved in insulin production as well as in adiponectin signaling and interacts specifically with the redox-regulatory endoplasmic reticulum proteins endoplasmic oxidoreductin 1alpha (Ero1alpha) and peroxiredoxin-4. Here, we show that ERp46, although lacking a PDI-like redox-inactive b'-thioredoxin domain with its hydrophobic substrate binding site, is able to bind to a large pool of peptides containing aromatic and basic residues via all three of its catalytic domains (a(0), a and a'), though the a(0) domain may contain the primary binding site. ERp46, which shows relatively higher activity as a disulfide-reductase than as an oxidase/isomerase in vitro compared to PDI and ERp57, possesses chaperone activity in vivo, a property also shared by the C-terminal a' domain. A crystal structure of the a' domain is also presented, offering a view of possible substrate binding sites within catalytic domains of PDI proteins. Peptide Binding by Catalytic Domains of the Protein Disulfide Isomerase-Related Protein ERp46.,Funkner A, Parthier C, Schutkowski M, Zerweck J, Lilie H, Gyrych N, Fischer G, Stubbs MT, Ferrari DM J Mol Biol. 2013 Jan 30. pii: S0022-2836(13)00045-4. doi:, 10.1016/j.jmb.2013.01.029. PMID:23376096[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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