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Article

The acidic C-terminal domain stabilizes the chaperone function of protein disulfide isomerase.

The Journal of biological chemistry - 19 Nov 2004

Tian Rui, Li Sheng-Jian, Wang Dong-Liang, Zhao Zhen, Liu Ying, He Rong-Qiao

Abstract excerpt

Protein disulfide isomerase (PDI, EC 5.3.4.1) is a chaperone and catalyzes the formation and rearrangement of disulfide bonds in proteins. Domain c-(463-491), containing 18 acidic residues, is an interesting and important C-terminal extension of PDI. In this study, the PDI mutant abb'a', in which domain c is truncated, was used to investigate the relationship between the C-terminal structure and chaperone...

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Identifiers

PMID: 15358778
DOI: 10.1074/jbc.M407076200

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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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