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Literature summary for 5.3.4.1 extracted from

  • Fu, X.; Zhu, B.T.
    Human pancreas-specific protein disulfide isomerase homolog (PDIp) is redox-regulated through formation of an inter-subunit disulfide bond (2009), Arch. Biochem. Biophys., 485, 1-9.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in COS-7 cells Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
isoform pancreas-specific protein disulfide isomerase homolog, PDIp
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information PDIp exists predominantly as monomer under reducing conditions, but the dimeric form is significantly increased following the removal of the reducing agent, due to the formation of an inter-subunit disulfide bond. The oxidized PDIp exposes more hydrophobic patches and is more sensitive to protease digestion. The formation of the inter-subunit disulfide bond is mainly contributed by its non-active cysteine residue C4. The formation of the inter-subunit disulfide bond is redox-dependent and is favored under oxidizing conditions. PDIp can function as a chaperone to form stable complexes with various non-native cellular proteins, particularly under oxidizing conditions Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
pancreas
-
Homo sapiens
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Subunits

Subunits Comment Organism
More PDIp exists predominantly as monomer under reducing conditions, but the dimeric form is significantly increased following the removal of the reducing agent, due to the formation of an inter-subunit disulfide bond. The oxidized PDIp exposes more hydrophobic patches and is more sensitive to protease digestion. The formation of the inter-subunit disulfide bond is mainly contributed by its non-active cysteine residue C4. The formation of the inter-subunit disulfide bond is redox-dependent and is favored under oxidizing conditions. PDIp can function as a chaperone to form stable complexes with various non-native cellular proteins, particularly under oxidizing conditions Homo sapiens