ArticleThe Journal of biological chemistry2010
Structural basis of cyclophilin B binding by the calnexin/calreticulin P-domain.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 98 citations in OpenAlex.
- Biophysical characterization of Cyclophilin B reveals membrane localization as its primary functional determinant as a prolyl isomerase.Protein science : a publication of the Protein Society · 2026Article
- N-glycan-dependent protein maturation and quality control in the ER.Nature reviews. Molecular cell biology · 2025Review
- Calreticulin-From the Endoplasmic Reticulum to the Plasma Membrane-Adventures of a Wandering Protein.Cancers · 2025Review
- Review
- The structural basis for the collagen processing by human P3H1/CRTAP/PPIB ternary complex.Nature communications · 2024Article
- Elucidating the zinc-binding proteome of Fusarium oxysporum f. sp. lycopersici with particular emphasis on zinc-binding effector proteins.Archives of microbiology · 2023Article
- Calnexin, More Than Just a Molecular Chaperone.Cells · 2023Review
- Intramembrane client recognition potentiates the chaperone functions of calnexin.The EMBO journal · 2022Article
- Mixed mechanism of conformational selection and induced fit as a molecular recognition process in the calreticulin family of proteins.PLoS computational biology · 2022Article
- Oligomannose-Type Glycan Processing in the Endoplasmic Reticulum and Its Importance in Misfolding Diseases.Biology · 2022Review
- Roles of Calreticulin in Protein Folding, Immunity, Calcium Signaling and Cell Transformation.Progress in molecular and subcellular biology · 2021Article
- Structural Analysis of Calreticulin, an Endoplasmic Reticulum-Resident Molecular Chaperone.Progress in molecular and subcellular biology · 2021Article
- Inorganic polyphosphate controls cyclophilin B-mediated collagen folding in osteoblast-like cells.The FEBS journal · 2020Article
- Calnexin cycle - structural features of the ER chaperone system.The FEBS journal · 2020Review
- Functional Innovation in the Evolution of the Calcium-Dependent System of the Eukaryotic Endoplasmic Reticulum.Frontiers in genetics · 2020Article
- A Roadmap for the Molecular Farming of Viral Glycoprotein Vaccines: Engineering Glycosylation and Glycosylation-Directed Folding.Frontiers in plant science · 2020Review
- Characterization of PPIB interaction in the P3H1 ternary complex and implications for its pathological mutations.Cellular and molecular life sciences : CMLS · 2019Article
- Protein Quality Control in the Endoplasmic Reticulum.The protein journal · 2019Review
- Article
- Single-particle electron microscopy structure of UDP-glucose:glycoprotein glucosyltransferase suggests a selectivity mechanism for misfolded proteins.The Journal of biological chemistry · 2017Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Little is known about how chaperones in the endoplasmic reticulum are organized into complexes to assist in the proper folding of secreted proteins. One notable exception is the complex of ERp57 and calnexin that functions as part the calnexin cycle to direct disulfide bond formation in N-glycoproteins. Here, we report three new complexes composed of the peptidyl prolyl cis-trans-isomerase cyclophilin B and any of the lectin chaperones: calnexin, calreticulin, or calmegin. The 1.7 Å crystal structure of cyclophilin with the proline-rich P-domain of calmegin reveals that binding is mediated by the same surface that binds ERp57. We used NMR titrations and mutagenesis to measure low micromolar binding of cyclophilin to all three lectin chaperones and identify essential interfacial residues. The immunosuppressant cyclosporin A did not affect complex formation, confirming the functional independence of the P-domain binding and proline isomerization sites of cyclophilin. Our results reveal the P-domain functions as a unique protein-protein interaction domain and implicate a peptidyl prolyl isomerase as a new element in the calnexin cycle.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.