| Replacement of domain b of human protein disulfide isomerase-related protein with domain b' of human protein disulfide isomerase dramatically increases its chaperone activity. | |
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MedLine Citation:
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PMID: 15147915 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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We have reported that human protein disulfide isomerase-related protein (hPDIR) has isomerase and chaperone activities that are lower than those of the human protein disulfide isomerase (hPDI), and that the b domain of hPDIR is critical for its chaperone activity [J. Biol. Chem. 279 (2004) 4604]. To investigate the basis of the differences between hPDI and hPDIR, and to determine the functions of each hPDIR domain in detail, we constructed several hPDIR domain mutants. Interestingly, when the b domain of hPDIR was replaced with the b' domain of hPDI, a dramatic increase in chaperone activity that was close to that of hPDI itself was observed. However, this mutant showed decreased oxidative refolding of alpha1-antitrypsin. The replacement of the b domain of hPDIR with the c domain of hPDI also increased its chaperone activity. These observations suggest that putative peptide-binding sites of hPDI determine both its chaperone activity and its substrate specificity. |
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Authors:
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Tomohisa Horibe; Daisuke Iguchi; Toshio Masuoka; Mitsuhiro Gomi; Taiji Kimura; Masakazu Kikuchi |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: FEBS letters Volume: 566 ISSN: 0014-5793 ISO Abbreviation: FEBS Lett. Publication Date: 2004 May |
Date Detail:
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Created Date: 2004-05-18 Completed Date: 2004-07-16 Revised Date: 2008-11-21 |
Medline Journal Info:
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Nlm Unique ID: 0155157 Medline TA: FEBS Lett Country: Netherlands |
Other Details:
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Languages: eng Pagination: 311-5 Citation Subset: IM |
Affiliation:
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Department of Bioscience and Technology, Faculty of Science and Engineering, Ritsumeikan University, 1-1-1 Noji-higashi, Kusatsu, Shiga, 525-8577, Japan. |
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Motifs Amino Acid Sequence Escherichia coli / genetics, metabolism Humans Molecular Chaperones / chemistry*, genetics, metabolism* Molecular Sequence Data Mutation Oxidation-Reduction Protein Disulfide-Isomerases / chemistry*, genetics, metabolism* Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Proteins / chemistry*, genetics, metabolism* Recombinant Proteins / chemistry, genetics, metabolism Spectrometry, Fluorescence |
| Chemical | |
Reg. No./Substance:
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0/Molecular Chaperones; 0/PDIR protein, human; 0/Proteins; 0/Recombinant Proteins; EC 5.3.4.1/Protein Disulfide-Isomerases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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