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Article

Mutations that destabilize the a' domain of human protein-disulfide isomerase indirectly affect peptide binding.

The Journal of biological chemistry - 5 May 2000

Klappa P, Koivunen P, Pirneskoski A, Karvonen P, Ruddock L W, Kivirikko K I, Freedman R B

Abstract excerpt

Protein-disulfide isomerase (PDI) is a catalyst of folding of disulfide-bonded proteins and also a multifunctional polypeptide that acts as the beta-subunit in the prolyl 4-hydroxylase alpha(2)beta(2)-tetramer (P4H) and the microsomal triglyceride transfer protein alphabeta-dimer. The principal peptide-binding site of PDI is located in the b' domain, but all domains contribute to the binding of misfolded...

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Identifiers

PMID: 10788425
DOI: 10.1074/jbc.275.18.13213

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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