Structural Characterization of Phosducin and its Complex with the 14-3-3 Protein
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11320%2F15%3A10294545" target="_blank" >RIV/00216208:11320/15:10294545 - isvavai.cz</a>
Nalezeny alternativní kódy
RIV/67985823:_____/15:00446984 RIV/61388971:_____/15:00446984 RIV/00216208:11310/15:10294545
Výsledek na webu
<a href="http://www.jbc.org/content/early/2015/05/13/jbc.M115.636563.full.pdf" target="_blank" >http://www.jbc.org/content/early/2015/05/13/jbc.M115.636563.full.pdf</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1074/jbc.M115.636563" target="_blank" >10.1074/jbc.M115.636563</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Structural Characterization of Phosducin and its Complex with the 14-3-3 Protein
Popis výsledku v původním jazyce
Background: Phosducin is a conserved regulatory phosphoprotein involved in phototransduction whose function is regulated in a 14-3-3-dependent manner. Results: The 14-3-3 protein binding affects the structure and the accessibility of several regions within both domains of phosphorylated phosducin. Conclusion: The 14-3-3 protein sterically occludes the whole G(t) binding interface of phosducin. Significance: Mechanistic explanation is given for the 14-3-3-dependent inhibition of phosducin function. Phosducin (Pdc), a highly conserved phosphoprotein involved in the regulation of retinal phototransduction cascade, transcriptional control, and modulation of blood pressure, is controlled in a phosphorylation-dependent manner, including the binding to the 14-3-3 protein. However, the molecular mechanism of this regulation is largely unknown. Here, the solution structure of Pdc and its interaction with the 14-3-3 protein were investigated using small angle x-ray scattering, time-resolved fluo
Název v anglickém jazyce
Structural Characterization of Phosducin and its Complex with the 14-3-3 Protein
Popis výsledku anglicky
Background: Phosducin is a conserved regulatory phosphoprotein involved in phototransduction whose function is regulated in a 14-3-3-dependent manner. Results: The 14-3-3 protein binding affects the structure and the accessibility of several regions within both domains of phosphorylated phosducin. Conclusion: The 14-3-3 protein sterically occludes the whole G(t) binding interface of phosducin. Significance: Mechanistic explanation is given for the 14-3-3-dependent inhibition of phosducin function. Phosducin (Pdc), a highly conserved phosphoprotein involved in the regulation of retinal phototransduction cascade, transcriptional control, and modulation of blood pressure, is controlled in a phosphorylation-dependent manner, including the binding to the 14-3-3 protein. However, the molecular mechanism of this regulation is largely unknown. Here, the solution structure of Pdc and its interaction with the 14-3-3 protein were investigated using small angle x-ray scattering, time-resolved fluo
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
CE - Biochemie
OECD FORD obor
—
Návaznosti výsledku
Projekt
<a href="/cs/project/GAP305%2F11%2F0708" target="_blank" >GAP305/11/0708: Úloha proteinu 14-3-3 na regulaci funkce fosducinu</a><br>
Návaznosti
S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2015
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Journal of Biological Chemistry
ISSN
0021-9258
e-ISSN
—
Svazek periodika
290
Číslo periodika v rámci svazku
26
Stát vydavatele periodika
US - Spojené státy americké
Počet stran výsledku
15
Strana od-do
16246-16260
Kód UT WoS článku
000356930100028
EID výsledku v databázi Scopus
2-s2.0-84941312517