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Article

Distinct contributions of the lectin and arm domains of calnexin to its molecular chaperone function.

The Journal of biological chemistry - 6 Feb 2009

Brockmeier Achim, Brockmeier Ulf, Williams David B

Abstract excerpt

Calnexin is a Ca2+-binding transmembrane chaperone of the endoplasmic reticulum that recognizes Glc1Man5-9GlcNAc2 oligosaccharides on folding glycoproteins as well as non-native elements of the polypeptide backbone. This latter mode of recognition enables calnexin to suppress the aggregation of both glycosylated and nonglycosylated substrates. The luminal portion of calnexin (S-Cnx) consists of two domains, a...

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Identifiers

PMID: 19074423
DOI: 10.1074/jbc.M804866200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Distinct contributions of the lectin and arm domains of calnexin to its molecular chaperone function.PMID 19074423Read ↗

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