Structural Characterization of Phosducin and its Complex with the 14-3-3 Protein
The result's identifiers
Result code in 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>
Alternative codes found
RIV/67985823:_____/15:00446984 RIV/61388971:_____/15:00446984 RIV/00216208:11310/15:10294545
Result on the web
<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>
Alternative languages
Result language
angličtina
Original language name
Structural Characterization of Phosducin and its Complex with the 14-3-3 Protein
Original language description
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
Czech name
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Czech description
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Classification
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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Result continuities
Project
<a href="/en/project/GAP305%2F11%2F0708" target="_blank" >GAP305/11/0708: Role of the 14-3-3 protein in the regulation of phosducin function</a><br>
Continuities
S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2015
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Biological Chemistry
ISSN
0021-9258
e-ISSN
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Volume of the periodical
290
Issue of the periodical within the volume
26
Country of publishing house
US - UNITED STATES
Number of pages
15
Pages from-to
16246-16260
UT code for WoS article
000356930100028
EID of the result in the Scopus database
2-s2.0-84941312517