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PDI-Regulated Disulfide Bond Formation in Protein Folding and Biomolecular Assembly
Disulfide bonds play a pivotal role in maintaining the natural structures of proteins to ensure their performance of normal biological functions. Moreover, biological molecular assembly, such as the gluten network, is also largely dependent on the intermolecular crosslinking via disulfide bonds. In...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7794689/ https://www.ncbi.nlm.nih.gov/pubmed/33396541 http://dx.doi.org/10.3390/molecules26010171 |
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author | Fu, Jiahui Gao, Jihui Liang, Zhongxin Yang, Dong |
author_facet | Fu, Jiahui Gao, Jihui Liang, Zhongxin Yang, Dong |
author_sort | Fu, Jiahui |
collection | PubMed |
description | Disulfide bonds play a pivotal role in maintaining the natural structures of proteins to ensure their performance of normal biological functions. Moreover, biological molecular assembly, such as the gluten network, is also largely dependent on the intermolecular crosslinking via disulfide bonds. In eukaryotes, the formation and rearrangement of most intra- and intermolecular disulfide bonds in the endoplasmic reticulum (ER) are mediated by protein disulfide isomerases (PDIs), which consist of multiple thioredoxin-like domains. These domains assist correct folding of proteins, as well as effectively prevent the aggregation of misfolded ones. Protein misfolding often leads to the formation of pathological protein aggregations that cause many diseases. On the other hand, glutenin aggregation and subsequent crosslinking are required for the formation of a rheologically dominating gluten network. Herein, the mechanism of PDI-regulated disulfide bond formation is important for understanding not only protein folding and associated diseases, but also the formation of functional biomolecular assembly. This review systematically illustrated the process of human protein disulfide isomerase (hPDI) mediated disulfide bond formation and complemented this with the current mechanism of wheat protein disulfide isomerase (wPDI) catalyzed formation of gluten networks. |
format | Online Article Text |
id | pubmed-7794689 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-77946892021-01-10 PDI-Regulated Disulfide Bond Formation in Protein Folding and Biomolecular Assembly Fu, Jiahui Gao, Jihui Liang, Zhongxin Yang, Dong Molecules Review Disulfide bonds play a pivotal role in maintaining the natural structures of proteins to ensure their performance of normal biological functions. Moreover, biological molecular assembly, such as the gluten network, is also largely dependent on the intermolecular crosslinking via disulfide bonds. In eukaryotes, the formation and rearrangement of most intra- and intermolecular disulfide bonds in the endoplasmic reticulum (ER) are mediated by protein disulfide isomerases (PDIs), which consist of multiple thioredoxin-like domains. These domains assist correct folding of proteins, as well as effectively prevent the aggregation of misfolded ones. Protein misfolding often leads to the formation of pathological protein aggregations that cause many diseases. On the other hand, glutenin aggregation and subsequent crosslinking are required for the formation of a rheologically dominating gluten network. Herein, the mechanism of PDI-regulated disulfide bond formation is important for understanding not only protein folding and associated diseases, but also the formation of functional biomolecular assembly. This review systematically illustrated the process of human protein disulfide isomerase (hPDI) mediated disulfide bond formation and complemented this with the current mechanism of wheat protein disulfide isomerase (wPDI) catalyzed formation of gluten networks. MDPI 2020-12-31 /pmc/articles/PMC7794689/ /pubmed/33396541 http://dx.doi.org/10.3390/molecules26010171 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Fu, Jiahui Gao, Jihui Liang, Zhongxin Yang, Dong PDI-Regulated Disulfide Bond Formation in Protein Folding and Biomolecular Assembly |
title | PDI-Regulated Disulfide Bond Formation in Protein Folding and Biomolecular Assembly |
title_full | PDI-Regulated Disulfide Bond Formation in Protein Folding and Biomolecular Assembly |
title_fullStr | PDI-Regulated Disulfide Bond Formation in Protein Folding and Biomolecular Assembly |
title_full_unstemmed | PDI-Regulated Disulfide Bond Formation in Protein Folding and Biomolecular Assembly |
title_short | PDI-Regulated Disulfide Bond Formation in Protein Folding and Biomolecular Assembly |
title_sort | pdi-regulated disulfide bond formation in protein folding and biomolecular assembly |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7794689/ https://www.ncbi.nlm.nih.gov/pubmed/33396541 http://dx.doi.org/10.3390/molecules26010171 |
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