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Article

Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase.

The Journal of biological chemistry - 12 Mar 2004

Pirneskoski Annamari, Klappa Peter, Lobell Mario, Williamson Richard A, Byrne Lee, Alanen Heli I, Salo Kirsi E H, Kivirikko Kari I, Freedman Robert B, Ruddock Lloyd W

Abstract excerpt

Disulfide bond formation in the endoplasmic reticulum of eukaryotes is catalyzed by the ubiquitously expressed enzyme protein disulfide isomerase (PDI). The effectiveness of PDI as a catalyst of native disulfide bond formation in folding polypeptides depends on the ability to catalyze disulfide-dithiol exchange, to bind non-native proteins, and to trigger conformational changes in the bound substrate, allowing...

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PMID: 14684740
DOI: 10.1074/jbc.M312193200

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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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