Biophysical and Structural Characterization of the Thioredoxin-binding Domain of Protein Kinase ASK1 and Its Interaction with Reduced Thioredoxin*

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F14%3A10271929" target="_blank" >RIV/00216208:11310/14:10271929 - isvavai.cz</a>
Alternative codes found
RIV/67985823:_____/14:00432569 RIV/00216208:11320/14:10271929
Result on the web
<a href="http://www.jbc.org/content/early/2014/07/17/jbc.M114.583807.full.pdf" target="_blank" >http://www.jbc.org/content/early/2014/07/17/jbc.M114.583807.full.pdf</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1074/jbc.M114.583807" target="_blank" >10.1074/jbc.M114.583807</a>

Result language
angličtina
Original language name
Biophysical and Structural Characterization of the Thioredoxin-binding Domain of Protein Kinase ASK1 and Its Interaction with Reduced Thioredoxin*
Original language description
Background: Thioredoxin is a physiological inhibitor of ASK1. Results: The catalytic motif of thioredoxin is essential for its binding to ASK1 and the interaction does not involve intermolecular disulfide bonds. Conclusion: Thioredoxin-binding domain ofASK1 is a rigid domain that interacts with reduced thioredoxin through a large binding interface. Significance: Structural basis of the interaction between ASK1 and reduced thioredoxin. Apoptosis signal-regulating kinase 1 (ASK1), a mitogen-activated protein kinase kinase kinase, plays a key role in the pathogenesis of multiple diseases. Its activity is regulated by thioredoxin (TRX1) but the precise mechanism of this regulation is unclear due to the lack of structural data. Here, we performed biophysical and structural characterization of the TRX1-binding domain of ASK1 (ASK1-TBD) and its complex with reduced TRX1. ASK1-TBD is a monomeric and rigid domain that forms a stable complex with reduced TRX1 with 1:1 molar stoichiometry. The b
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Project
<a href="/en/project/GA14-10061S" target="_blank" >GA14-10061S: Regulatory mechanism of kinase activity of protein kinase ASK1</a><br>
Continuities
S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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