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Article

Alternative conformations of the x region of human protein disulphide-isomerase modulate exposure of the substrate binding b' domain.

Journal of molecular biology - 28 Nov 2008

Nguyen Van Dat, Wallis Katrine, Howard Mark J, Haapalainen Antti M, Salo Kirsi E H, Saaranen Mirva J, Sidhu Ateesh, Wierenga Rik K, Freedman Robert B, Ruddock Lloyd W, Williamson Richard A

Abstract excerpt

Protein disulphide isomerase (PDI) is a key multi-domain protein folding catalyst in the endoplasmic reticulum. The b' domain of PDI is essential for the non-covalent binding of incompletely folded protein substrates. Earlier, we defined the substrate binding site in the b' domain of human PDI by modelling and mutagenesis studies. Here, we show by fluorescence and NMR that recombinant human PDI b'x (comprising...

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Identifiers

PMID: 18801374
DOI: 10.1016/j.jmb.2008.08.085

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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