Crystal structure of fully oxidized human thioredoxin
- Authors
- Hwang, Jungwon; Nguyen, Loi T.; Jeon, Young Ho; Lee, Chan Yong; Kim, Myung Hee
- Issue Date
- 13-11월-2015
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- Thioredoxin; Oxidoreductase; Redox; X-ray structure
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.467, no.2, pp.218 - 222
- Indexed
- SCIE
SCOPUS
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Volume
- 467
- Number
- 2
- Start Page
- 218
- End Page
- 222
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/91909
- DOI
- 10.1016/j.bbrc.2015.10.003
- ISSN
- 0006-291X
- 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.
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Collections - College of Pharmacy > Department of Pharmaceutical Science > 1. Journal Articles
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