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

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/67985823:_____/14:00432569 RIV/00216208:11320/14:10271929

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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

Název v anglickém jazyce

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

Popis výsledku anglicky

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

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/GA14-10061S" target="_blank" >GA14-10061S: Mechanismus regulace kinasové aktivity proteinkinasy ASK1</a><br>

Návaznosti

S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2014

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Biological Chemistry

ISSN

0021-9258

e-ISSN

—

Svazek periodika

289

Číslo periodika v rámci svazku

35

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

12

Strana od-do

24463-24474

Kód UT WoS článku

000341505600039

EID výsledku v databázi Scopus

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