[NMR paper] Characterization of residue-dependent differences in the peripheral membrane association of the FATC domain of the kinase 'target of rapamycin' by NMR and CD spectroscopy.
Characterization of residue-dependent differences in the peripheral membrane association of the FATC domain of the kinase 'target of rapamycin' by NMR and CD spectroscopy.
Related ArticlesCharacterization of residue-dependent differences in the peripheral membrane association of the FATC domain of the kinase 'target of rapamycin' by NMR and CD spectroscopy.
FEBS Lett. 2014 Apr 3;
Authors: Sommer LA, Dames SA
Abstract
The conserved C-terminal FATC domain of the kinase 'target of rapamycin' is important for its regulation and was suggested to contain a peripheral membrane anchor. Here, we present the characterization of the interactions of the yeast TOR1 FATC domain (2438-2470 = y1fatc) and 15 mutants with membrane mimetic micelles, bicelles, and small unilamellar vesicles (SUVs) by NMR and CD spectroscopy. Replacement of up to 6-7 residues did not result in a significant abrogation of the association with micelles or bicelles. However, replacement of only one residue could result in an impairment of the interaction with SUVs that are usually used at low concentrations. Some mutants not binding liposomes may be introduced in full-length TOR for future functional and localization studies in vivo.
PMID: 24704685 [PubMed - as supplied by publisher]
[NMR paper] Depletion of casein kinase I leads to a NAD(P)(+)/NAD(P)H balance-dependent metabolic adaptation as determined by NMR spectroscopy-metabolomic profile in Kluyveromyces lactis.
Depletion of casein kinase I leads to a NAD(P)(+)/NAD(P)H balance-dependent metabolic adaptation as determined by NMR spectroscopy-metabolomic profile in Kluyveromyces lactis.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Depletion of casein kinase I leads to a NAD(P)(+)/NAD(P)H balance-dependent metabolic adaptation as determined by NMR spectroscopy-metabolomic profile in Kluyveromyces lactis.
Biochim Biophys Acta. 2014 Jan;1840(1):556-64
Authors: Gorietti D, Zanni...
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NMR of Conditional Peripheral Membrane Proteins
NMR of Conditional Peripheral Membrane Proteins
Publication date: 28 January 2014
Source:Biophysical Journal, Volume 106, Issue 2, Supplement 1</br>
Author(s): Krystal A. Morales , Mikaela D. Stewart , Tatyana I. Igumenova</br>
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[NMR paper] NMR structure and MD simulations of the AAA protease intermembrane space domain indicates peripheral membrane localization within the hexaoligomer.
NMR structure and MD simulations of the AAA protease intermembrane space domain indicates peripheral membrane localization within the hexaoligomer.
NMR structure and MD simulations of the AAA protease intermembrane space domain indicates peripheral membrane localization within the hexaoligomer.
FEBS Lett. 2013 Sep 18;
Authors: Ramelot TA, Yang Y, Sahu ID, Lee HW, Xiao R, Lorigan GA, Montelione GT, Kennedy MA
Abstract
We have determined the solution NMR structure of the intermembrane space domain (IMSD) of the human mitochondrial...
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[NMR paper] NMR- and CD-Monitored Lipid-Binding Studies Suggest a General Role for the FATC Domain as Membrane Anchor of Phosphatidyl-Inositol-3 Kinase-Related Kinases (PIKKs).
NMR- and CD-Monitored Lipid-Binding Studies Suggest a General Role for the FATC Domain as Membrane Anchor of Phosphatidyl-Inositol-3 Kinase-Related Kinases (PIKKs).
Related Articles NMR- and CD-Monitored Lipid-Binding Studies Suggest a General Role for the FATC Domain as Membrane Anchor of Phosphatidyl-Inositol-3 Kinase-Related Kinases (PIKKs).
J Biol Chem. 2013 May 13;
Authors: Sommer LA, Schaad M, Dames SA
Abstract
The FATC domain is shared by all members of the family of phosphatidylinositol-3 kinase related kinases (PIKKs). It has been...
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[NMR paper] Residue-specific real-time NMR diffusion experiments define the association states of
Residue-specific real-time NMR diffusion experiments define the association states of proteins during folding.
Related Articles Residue-specific real-time NMR diffusion experiments define the association states of proteins during folding.
J Am Chem Soc. 2002 Jun 19;124(24):7156-62
Authors: Buevich AV, Baum J
Characterizing the association states of proteins during folding is critical for understanding the nature of protein-folding intermediates and protein-folding pathways, protein aggregation, and disease-related aggregation. To study the...
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[NMR paper] Phosphorylation and flexibility of cyclic-AMP-dependent protein kinase (PKA) using (3
Phosphorylation and flexibility of cyclic-AMP-dependent protein kinase (PKA) using (31)P NMR spectroscopy.
Related Articles Phosphorylation and flexibility of cyclic-AMP-dependent protein kinase (PKA) using (31)P NMR spectroscopy.
Biochemistry. 2002 May 14;41(19):5968-77
Authors: Seifert MH, Breitenlechner CB, Bossemeyer D, Huber R, Holak TA, Engh RA
Cell signaling pathways rely on phosphotransfer reactions that are catalyzed by protein kinases. The protein kinases themselves are typically regulated by phosphorylation and concurrent structural...
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[NMR paper] Isoform-specific differences between the type Ialpha and IIalpha cyclic AMP-dependent
Isoform-specific differences between the type Ialpha and IIalpha cyclic AMP-dependent protein kinase anchoring domains revealed by solution NMR.
Related Articles Isoform-specific differences between the type Ialpha and IIalpha cyclic AMP-dependent protein kinase anchoring domains revealed by solution NMR.
J Biol Chem. 2000 Nov 10;275(45):35146-52
Authors: Banky P, Newlon MG, Roy M, Garrod S, Taylor SS, Jennings PA
Cyclic AMP dependent protein kinase (PKA) is controlled, in part, by the subcellular localization of the enzyme (). Discovery of...
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[NMR paper] Solvent polarity-dependent structural refolding: a CD and NMR study of a 15 residue p
Solvent polarity-dependent structural refolding: a CD and NMR study of a 15 residue peptide.
Related Articles Solvent polarity-dependent structural refolding: a CD and NMR study of a 15 residue peptide.
Proteins. 1995 Oct;23(2):196-203
Authors: Graf von Stosch A, Jiménez MA, Kinzel V, Reed J
A close association between the HIV surface protein gp120 and the CD4 T cell receptor initiates the viral multiplication cycle. A 15 amino acid peptide (LAV) within the CD4 binding domain of gp 120 has been shown to retain receptor binding ability. The...
Characterization of residue-dependent differences in the peripheral membrane association of the FATC domain of the kinase 'target of rapamycin' by NMR and CD spectroscopy.
Linear Mode
