Dissection of Binding between a Phosphorylated Tyrosine Hydroxylase Peptide and 14-3-3zéta: A Complex Story Elucidated by NMR
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F14%3A00077266" target="_blank" >RIV/00216224:14740/14:00077266 - isvavai.cz</a>
Result on the web
<a href="http://www.sciencedirect.com/science/article/pii/S0006349514010121" target="_blank" >http://www.sciencedirect.com/science/article/pii/S0006349514010121</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.bpj.2014.08.039" target="_blank" >10.1016/j.bpj.2014.08.039</a>
Alternative languages
Result language
angličtina
Original language name
Dissection of Binding between a Phosphorylated Tyrosine Hydroxylase Peptide and 14-3-3zéta: A Complex Story Elucidated by NMR
Original language description
Human tyrosine hydroxylase activity is regulated by phosphorylation of its N-terminus and by an interaction with the modulator 14-3-3 proteins. We investigated the binding of singly or doubly phosphorylated and thiophosphorylated peptides, comprising thefirst 50 amino acids of human tyrosine hydroxylase, isoform 1 (hTH1), that contain the critical interaction domain, to 14-3-3zéta, by 31P NMR. Single phosphorylation at S19 generates a high affinity 14-3-3zéta binding epitope, whereas singly S40-phosphorylated peptide interacts with 14-3-3zéta one order-of-magnitude weaker than the S19-phosphorylated peptide.
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
BO - Biophysics
OECD FORD branch
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Result continuities
Project
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Continuities
R - Projekt Ramcoveho programu EK
Others
Publication year
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Biophysical Journal
ISSN
0006-3495
e-ISSN
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Volume of the periodical
107
Issue of the periodical within the volume
9
Country of publishing house
US - UNITED STATES
Number of pages
10
Pages from-to
2185-2194
UT code for WoS article
000344232500020
EID of the result in the Scopus database
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