Related ArticlesPhosphorylation of the regulatory domain of human tyrosine hydroxylase 1 monitored using non-uniformly sampled NMR.
Biophys Chem. 2017 Jan 27;223:25-29
Authors: Louša P, Nedozrálová H, Župa E, Nová?ek J, Hritz J
Abstract
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.
PMID: 28282625 [PubMed - as supplied by publisher]
Accurate determination of rates from non-uniformly sampled relaxation data
Accurate determination of rates from non-uniformly sampled relaxation data
Abstract
The application of non-uniform sampling (NUS) to relaxation experiments traditionally used to characterize the fast internal motion of proteins is quantitatively examined. Experimentally acquired Poisson-gap sampled data reconstructed with iterative soft thresholding are compared to regular sequentially sampled (RSS) data. Using ubiquitin as a model system, it is shown that 25Â*% sampling is sufficient for the determination of quantitatively accurate relaxation...
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[NMR paper] Dissection of Binding between a Phosphorylated Tyrosine Hydroxylase Peptide and 14-3-3?: A Complex Story Elucidated by NMR.
Dissection of Binding between a Phosphorylated Tyrosine Hydroxylase Peptide and 14-3-3?: A Complex Story Elucidated by NMR.
Dissection of Binding between a Phosphorylated Tyrosine Hydroxylase Peptide and 14-3-3?: A Complex Story Elucidated by NMR.
Biophys J. 2014 Nov 4;107(9):2185-94
Authors: Hritz J, Byeon IJ, Krzysiak T, Martinez A, Sklenar V, Gronenborn AM
Abstract
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...
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11-25-2014 09:40 PM
[NMR paper] Unraveling a phosphorylation event in a folded protein by NMR spectroscopy: phosphorylation of the Pin1 WW domain by PKA.
Unraveling a phosphorylation event in a folded protein by NMR spectroscopy: phosphorylation of the Pin1 WW domain by PKA.
Unraveling a phosphorylation event in a folded protein by NMR spectroscopy: phosphorylation of the Pin1 WW domain by PKA.
J Biomol NMR. 2013 Mar 2;
Authors: Smet-Nocca C, Launay H, Wieruszeski JM, Lippens G, Landrieu I
Abstract
The Pin1 protein plays a critical role in the functional regulation of the hyperphosphorylated neuronal Tau protein in Alzheimer's disease and is by itself regulated by phosphorylation. We have...
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03-05-2013 03:25 PM
[NMR paper] A Genetically Encoded 19 F NMR Probe for Tyrosine Phosphorylation.
A Genetically Encoded 19 F NMR Probe for Tyrosine Phosphorylation.
A Genetically Encoded 19 F NMR Probe for Tyrosine Phosphorylation.
Angew Chem Int Ed Engl. 2013 Feb 28;
Authors: Li F, Shi P, Li J, Yang F, Wang T, Zhang W, Gao F, Ding W, Li D, Li J, Xiong Y, Sun J, Gong W, Tian C, Wang J
Abstract
Simple and selective: Tyrosine phosphorylation is a pivotal post-translational modification which regulates the enzymatic activity, protein conformation, and protein-protein interactions. The highly efficient genetic incorporation of...
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03-02-2013 11:45 AM
[NMR paper] NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 1.
NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 1.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 1.
Biomol NMR Assign. 2013 Jan 17;
Authors: Vajpai N, Schott AK, Vogtherr M, Breeze AL
Abstract
Members of the fibroblast growth factor receptor tyrosine kinase family (FGFR1-4) play an important role in many...
Analysis of non-uniformly sampled spectra with multi-dimensional decomposition
Analysis of non-uniformly sampled spectra with multi-dimensional decomposition
Publication year: 2011
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volume 59, Issue 3</br>
Vladislav Yu. Orekhov, Victor A. Jaravine</br>
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Phosphorylation of the regulatory domain of human tyrosine hydroxylase 1 monitored using non-uniformly sampled NMR.
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