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== 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). | [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). | ||
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== Publication Abstract from PubMed == | |||
The 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<ref>PMID:23376096</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 3uj1" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[ER-resident protein|ER-resident protein]] | *[[ER-resident protein|ER-resident protein]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
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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