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Article

Structural basis of cyclophilin B binding by the calnexin/calreticulin P-domain.

The Journal of biological chemistry - 12 Nov 2010

Kozlov Guennadi, Bastos-Aristizabal Sara, Määttänen Pekka, Rosenauer Angelika, Zheng Fenglin, Killikelly April, Trempe Jean-François, Thomas David Y, Gehring Kalle

Abstract excerpt

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...

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Identifiers

PMID: 20801878
DOI: 10.1074/jbc.M110.160101
PMCID: PMC2975179

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural basis of cyclophilin B binding by the calnexin/calreticulin P-domain.PMID 20801878Read ↗

Mapping the ER Interactome: The P Domains of Calnexin and Calreticulin as Plurivalent Adapters for Foldases and Chaperones.Semantic proximity Read ↗

Substrate specificity of the oxidoreductase ERp57 is determined primarily by its interaction with calnexin and calreticulin.Semantic proximity Read ↗

Calnexin, calreticulin, and Bip/Kar2p in protein folding.Semantic proximity Read ↗

Lectin-deficient calnexin is capable of binding class I histocompatibility molecules in vivo and preventing their degradation.Semantic proximity Read ↗

Contrasting Functions of Calreticulin and Calnexin in Glycoprotein Folding and ER Quality ControlSemantic proximity Read ↗

Calreticulin and calnexin interact with different protein and glycan determinants during the assembly of MHC class I.Semantic proximity Read ↗

Mutational analysis of calnexin.Semantic proximity Read ↗

Calreticulin mutations affect its chaperone function and perturb the glycoproteome.Semantic proximity Read ↗

Identification by mutational analysis of amino acid residues essential in the chaperone function of calreticulin.Semantic proximity Read ↗

The polypeptide binding conformation of calreticulin facilitates its cell-surface expression under conditions of endoplasmic reticulum stress.Semantic proximity Read ↗

Mpl is activated by dimers of MPN-linked calreticulin mutants stabilized by disulfide bonds and ionic interactionsSemantic proximity Read ↗

Calnexin recognizes carbohydrate and protein determinants of class I major histocompatibility complex molecules.Semantic proximity Read ↗

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