ArticleScientific reports2015
Structural basis of redox-dependent substrate binding of protein disulfide isomerase.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 31 citations in OpenAlex.
- Transient Interactions of α-Synuclein N- and C-Termini.ACS chemical neuroscience · 2026Article
- Molecular Design of FRET Probes Based on Domain Rearrangement of Protein Disulfide Isomerase for Monitoring Intracellular Redox Status.International journal of molecular sciences · 2023Article
- C-terminal truncation modulates α-Synuclein's cytotoxicity and aggregation by promoting the interactions with membrane and chaperone.Communications biology · 2022Article
- Conformational Variability of Amyloid-β and the Morphological Diversity of Its Aggregates.Molecules (Basel, Switzerland) · 2022Review
- Neurons and Glia Interplay in α-Synucleinopathies.International journal of molecular sciences · 2021Review
- PDI-Regulated Disulfide Bond Formation in Protein Folding and Biomolecular Assembly.Molecules (Basel, Switzerland) · 2020Review
- Stability and Conformational Resilience of Protein Disulfide Isomerase.Biochemistry · 2019Article
- The crystal structure of human microsomal triglyceride transfer protein.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Modelling of substrate access and substrate binding to cephalosporin acylases.Scientific reports · 2019Article
- Design, Synthesis, and Biological Evaluation of Novel Allosteric Protein Disulfide Isomerase Inhibitors.Journal of medicinal chemistry · 2019Article
- Inhibition of protein disulfide isomerase in glioblastoma causes marked downregulation of DNA repair and DNA damage response genes.Theranostics · 2019Article
- Cryo-EM structure of alpha-synuclein fibrils.eLife · 2018Article
- Molecular basis of rutin inhibition of protein disulfide isomerase (PDI) by combinedRSC advances · 2018Article
- Chemistry and Enzymology of Disulfide Cross-Linking in Proteins.Chemical reviews · 2018Review
- 'Something in the way she moves': The functional significance of flexibility in the multiple roles of protein disulfide isomerase (PDI).Biochimica et biophysica acta. Proteins and proteomics · 2017Review
- Machine Learning and Network Analysis of Molecular Dynamics Trajectories Reveal Two Chains of Red/Ox-specific Residue Interactions in Human Protein Disulfide Isomerase.Scientific reports · 2017Article
- Article
- Protein Partners of α-Synuclein in Health and Disease.Brain pathology (Zurich, Switzerland) · 2016Review
- Combined ligand-observe (19)F and protein-observe (15)N,(1)H-HSQC NMR suggests phenylalanine as the key Δ-somatostatin residue recognized by human protein disulfide isomerase.Scientific reports · 2016Article
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein disulfide isomerase (PDI) is a multidomain enzyme, operating as an essential folding catalyst, in which the b' and a' domains provide substrate binding sites and undergo an open-closed domain rearrangement depending on the redox states of the a' domain. Despite the long research history of this enzyme, three-dimensional structural data remain unavailable for its ligand-binding mode. Here we characterize PDI substrate recognition using α-synuclein (αSN) as the model ligand. Our nuclear magnetic resonance (NMR) data revealed that the substrate-binding domains of PDI captured the αSN segment Val37-Val40 only in the oxidized form. Furthermore, we determined the crystal structure of an oxidized form of the b'-a' domains in complex with an undecapeptide corresponding to this segment. The peptide-binding mode observed in the crystal structure with NMR validation, was characterized by hydrophobic interactions on the b' domain in an open conformation. Comparison with the previously reported crystal structure indicates that the a' domain partially masks the binding surface of the b' domain, causing steric hindrance against the peptide in the reduced form of the b'-a' domains that exhibits a closed conformation. These findings provide a structural basis for the mechanism underlying the redox-dependent substrate binding of PDI.
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