Crystal structure of fully oxidized human thioredoxin
DC Field | Value | Language |
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dc.contributor.author | Hwang, Jungwon | - |
dc.contributor.author | Nguyen, Loi T. | - |
dc.contributor.author | Jeon, Young Ho | - |
dc.contributor.author | Lee, Chan Yong | - |
dc.contributor.author | Kim, Myung Hee | - |
dc.date.accessioned | 2021-09-04T10:35:56Z | - |
dc.date.available | 2021-09-04T10:35:56Z | - |
dc.date.created | 2021-06-10 | - |
dc.date.issued | 2015-11-13 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/91909 | - |
dc.description.abstract | In addition to the active cysteines located at positions 32 and 35 in humans, mammalian cytosolic thioredoxin (TRX) possesses additional conserved cysteine residues at positions 62, 69, and 73. These non-canonical cysteine residues, that are distinct from prokaryotic TRX and also not found in mammalian mitochondrial TRX, have been implicated in biological functions regulating signal transduction pathways via their post-translational modifications. Here, we describe for the first time the structure of a fully oxidized TRX. The structure shows a non-active Cys62-Cys69 disulfide bond in addition to the active Cys32-Cys35 disulfide. The non-active disulfide switches the alpha 3-helix of TRX, composed of residues Cys62 to Glu70, to a bulging loop and dramatically changes the environment of the TRX residues involved in the interaction with its reductase and other cellular substrates. This structural modification may have implications for a number of potential functions of TRX including the regulation of redox-dependent signaling pathways. (C) 2015 Elsevier Inc. All rights reserved. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.subject | NF-KAPPA-B | - |
dc.subject | REDUCTASE | - |
dc.subject | GLUTATHIONE | - |
dc.subject | COMPLEX | - |
dc.title | Crystal structure of fully oxidized human thioredoxin | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Jeon, Young Ho | - |
dc.identifier.doi | 10.1016/j.bbrc.2015.10.003 | - |
dc.identifier.scopusid | 2-s2.0-84944385243 | - |
dc.identifier.wosid | 000364437700007 | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.467, no.2, pp.218 - 222 | - |
dc.relation.isPartOf | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.title | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.volume | 467 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 218 | - |
dc.citation.endPage | 222 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.subject.keywordPlus | NF-KAPPA-B | - |
dc.subject.keywordPlus | REDUCTASE | - |
dc.subject.keywordPlus | GLUTATHIONE | - |
dc.subject.keywordPlus | COMPLEX | - |
dc.subject.keywordAuthor | Thioredoxin | - |
dc.subject.keywordAuthor | Oxidoreductase | - |
dc.subject.keywordAuthor | Redox | - |
dc.subject.keywordAuthor | X-ray structure | - |
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