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Thioredoxin A active-site mutants form mixed disulfide dimers that resemble enzyme-substrate reaction intermediates.

Abstract:

Thioredoxin functions in nearly all organisms as the major thiol-disulfide oxidoreductase within the cytosol. Its prime purpose is to maintain cysteine-containing proteins in the reduced state by converting intramolecular disulfide bonds into dithiols in a disulfide exchange reaction. Thioredoxin has been reported to contribute to a wide variety of physiological functions by interacting with specific sets of substrates in different cell types. To investigate the function of the essential thio...

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Publication status:
Published

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Publisher copy:
10.1016/j.jmb.2008.03.077

Authors


Kouwen, TR More by this author
Andréll, J More by this author
Schrijver, R More by this author
Dubois, JY More by this author
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Journal:
Journal of molecular biology
Volume:
379
Issue:
3
Pages:
520-534
Publication date:
2008-06-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:65674f77-5bb5-4f55-a0e8-623ab67913c3
Source identifiers:
72812
Local pid:
pubs:72812

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