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Article

Lectin-deficient calreticulin retains full functionality as a chaperone for class I histocompatibility molecules.

Molecular biology of the cell - 1 Jun 2008

Ireland Breanna S, Brockmeier Ulf, Howe Christopher M, Elliott Tim, Williams David B

Abstract excerpt

Calreticulin is a molecular chaperone of the endoplasmic reticulum that uses both a lectin site specific for Glc(1)Man(5-9)GlcNAc(2) oligosaccharides and a polypeptide binding site to interact with nascent glycoproteins. The latter mode of substrate recognition is controversial. To examine the relevance of polypeptide binding to protein folding in living cells, we prepared lectin-deficient mutants of calreticulin...

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Identifiers

PMID: 18337472
DOI: 10.1091/mbc.e07-10-1055
PMCID: PMC2397311

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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.

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