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Phosphorylation of the regulatory domain of human tyrosine hydroxylase 1 monitored using non-uniformly sampled NMR
P. Louša, H. Nedozrálová, E. Župa, J. Nováček, J. Hritz,
Jazyk angličtina Země Nizozemsko
Typ dokumentu časopisecké články
- MeSH
- fosforylace MeSH
- intracelulární signální peptidy a proteiny metabolismus MeSH
- kinetika MeSH
- lidé MeSH
- magnetická rezonanční spektroskopie metody MeSH
- protein-serin-threoninkinasy metabolismus MeSH
- proteinkinasy závislé na cyklickém AMP metabolismus MeSH
- proteinové domény MeSH
- sekundární struktura proteinů MeSH
- tyrosin-3-monooxygenasa chemie metabolismus MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
Human tyrosine hydroxylase 1 (hTH1) activity is regulated by phosphorylation of its regulatory domain (RD-hTH1) and by an interaction with the 14-3-3 protein. The RD-hTH1 is composed of a structured region (66-169) preceded by an intrinsically disordered protein region (IDP, hTH1_65) containing two phosphorylation sites (S19 and S40) which are highly relevant for its increase in activity. The NMR signals of the IDP region in the non-phosphorylated, singly phosphorylated (pS40) and doubly phosphorylated states (pS19_pS40) were assigned by non-uniformly sampled spectra with increased dimensionality (5D). The structural changes induced by phosphorylation were analyzed by means of secondary structure propensities. The phosphorylation kinetics of the S40 and S19 by kinases PKA and PRAK respectively were monitored by non-uniformly sampled time-resolved NMR spectroscopy followed by their quantitative analysis.
Citace poskytuje Crossref.org
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