ArticlePloS one2013
Structure of the non-catalytic domain of the protein disulfide isomerase-related protein (PDIR) reveals function in protein binding.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Calreticulin-From the Endoplasmic Reticulum to the Plasma Membrane-Adventures of a Wandering Protein.Cancers · 2025Review
- Article
- Redox proteomics and structural analyses provide insightful implications for additional non-catalytic thiol-disulfide motifs in PDIs.Redox biology · 2023Article
- Interaction of Destruxin A with Three Silkworm Proteins: BmCRT, BmDPP3, and BmPDIA5.Molecules (Basel, Switzerland) · 2022Article
- Circulating protein disulfide isomerase family member 4 is associated with type 2 diabetes mellitus, insulin sensitivity, and obesity.Acta diabetologica · 2022Article
- Pan-Cancer Analysis of the Immunological Role of PDIA5: A Potential Target for Immunotherapy.Frontiers in immunology · 2022Article
- PDIA5 is Correlated With Immune Infiltration and Predicts Poor Prognosis in Gliomas.Frontiers in immunology · 2021Article
- Calnexin cycle - structural features of the ER chaperone system.The FEBS journal · 2020Review
- Review
- ABHD5 blunts the sensitivity of colorectal cancer to fluorouracil via promoting autophagic uracil yield.Nature communications · 2019Article
- Interdomain conformational flexibility underpins the activity of UGGT, the eukaryotic glycoprotein secretion checkpoint.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Emerging roles of protein disulfide isomerase in cancer.BMB reports · 2017Review
- Identification of six polymorphisms as novel susceptibility loci for ischemic or hemorrhagic stroke by exome-wide association studies.International journal of molecular medicine · 2017Article
- Calreticulin: Challenges Posed by the Intrinsically Disordered Nature of Calreticulin to the Study of Its Function.Frontiers in cell and developmental biology · 2017Article
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Authors and funding
3 authors.
Funding
Abstract
Protein disulfide isomerases comprise a large family of enzymes responsible for catalyzing the proper oxidation and folding of newly synthesized proteins in the endoplasmic reticulum (ER). Protein disulfide isomerase-related (PDIR) protein (also known as PDIA5) is a specialized member that participates in the folding of α1-antitrypsin and N-linked glycoproteins. Here, the crystal structure of the non-catalytic domain of PDIR was determined to 1.5 Å resolution. The structure adopts a thioredoxin-like fold stabilized by a structural disulfide bridge with a positively charged binding surface for interactions with the ER chaperones, calreticulin and ERp72. Crystal contacts between molecules potentially mimic the interactions of PDIR with misfolded substrate proteins. The results suggest that the non-catalytic domain of PDIR plays a key role in the recognition of protein partners and substrates.
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