CH-? interaction in VQIVYK sequence elucidated by NMR spectroscopy is essential for PHF formation of tau.
Biopolymers. 2014 Mar 29;
Authors: Sogawa K, Minoura K, In Y, Ishida T, Taniguchi T, Tomoo K
Abstract
One of the histopathological features of Alzheimer's disease (AD) is higher order neurofibrillary tangles formed by abnormally aggregated tau protein. Investigation of the mechanism of tau aggregation is important for the clarifying the cause of AD and the development of therapeutic drugs. The microtubule-binding domain (MBD) which consists of repeats of similar amino acids (R1-R4) is thought to form the core component of paired helical filament (PHF). The hexapeptide (306) VQIVYK(311) of R3 has been shown to take a key role of promoting tau aggregation and assumed that its CH-? interaction between the side chains of Ile308 and Tyr310 would contribute in stabilizing the filament. In this work, we investigated a short isoform of tau (4RTau), R3, VQIVYK peptide and their mutants by thioflavin S (ThS) fluorescence, and NMR measurements, and proved for the first time that this CH-? interaction stabilizes the filament at the atomic level. In addition, by molecular modeling, we revealed that this interaction further supports an extended amphipathic structure for molecular self-association during the process of PHF formation of tau protein. The present work indicates new approach that inhibits the CH-? interaction for developing a therapeutic agent for AD.
PMID: 24687309 [PubMed - as supplied by publisher]
[NMR paper] Protein dynamics elucidated by NMR technique.
Protein dynamics elucidated by NMR technique.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Protein dynamics elucidated by NMR technique.
Protein Cell. 2013 Oct;4(10):726-730
Authors: Li C, Tang C, Liu M
PMID: 24104391
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[NMR paper] NMR Solution Structure and SRP54M predicted interaction of the N-Terminal sequence (1-30) of the ovine Doppel protein.
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http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR Solution Structure and SRP54M predicted interaction of the N-Terminal sequence (1-30) of the ovine Doppel protein.
Peptides. 2013 Aug 22;
Authors: Pimenta J, Viegas A, Sardinha J, Martins IC, Cabrita EJ, Fontes CM, Prates JA, Pereira RM
Abstract
Prion protein (PrP(C))...
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NMR Solution Structure and SRP54M predicted interaction of the N-Terminal sequence (1-30) of the ovine Doppel protein
NMR Solution Structure and SRP54M predicted interaction of the N-Terminal sequence (1-30) of the ovine Doppel protein
Publication date: Available online 22 August 2013
Source:Peptides</br>
Author(s): Jorge Pimenta , Aldino Viegas , João Sardinha , Ivo C. Martins , Eurico J. Cabrita , Carlos M.G.A. Fontes , José A. Prates , Rosa M.L.N. Pereira</br>
Prion protein (PrPC) biosynthesis involves a multi-step process that includes translation and post-translational modifications. While PrP has been widely investigated, for the homolog Doppel (Dpl), limited knowledge...
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08-23-2013 01:07 AM
Role of Hydrophobic Interactions in the EncounterComplex Formation of the Plastocyanin and Cytochrome f Complex Revealed by Paramagnetic NMR Spectroscopy
Role of Hydrophobic Interactions in the EncounterComplex Formation of the Plastocyanin and Cytochrome f Complex Revealed by Paramagnetic NMR Spectroscopy
Sandra Scanu, Johannes M. Foerster, G. Matthias Ullmann and Marcellus Ubbink
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja4015452/aop/images/medium/ja-2013-015452_0009.gif
Journal of the American Chemical Society
DOI: 10.1021/ja4015452
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http://feeds.feedburner.com/~r/acs/jacsat/~4/I9ARcKlvRs8
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Sequence-Specific Mappingof the Interaction betweenUrea and Unfolded Ubiquitin from Ensemble Analysis of NMR and SmallAngle Scattering Data
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Jie-rong Huang, Frank Gabel, Malene Ringkjøbing Jensen, Stephan Grzesiek and Martin Blackledge
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2118688/aop/images/medium/ja-2011-118688_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2118688
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http://feeds.feedburner.com/~r/acs/jacsat/~4/u0K4iYUlStc
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[NMR paper] Interaction of the human prion PrP(106-126) sequence with copper(II), manganese(II),
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J Am Chem Soc. 2005 Jan 26;127(3):996-1006
Authors: Gaggelli E, Bernardi F, Molteni E, Pogni R, Valensin D, Valensin G, Remelli M, Luczkowski M, Kozlowski H
The synthetic peptide encompassing residues 106-126 (PrP106-126, KTNMKHMAGAAAAGAVVGGLG) of the human prion protein was considered for...
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[NMR paper] NMR solution structure and membrane interaction of the N-terminal sequence (1-30) of
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Authors: Biverståhl H, Andersson A, Gräslund A, Mäler L
The structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein (bPrPp) has been investigated by NMR spectroscopy in phospholipid membrane mimetic systems. CD spectroscopy...
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[NMR paper] Three-dimensional solid-state NMR spectroscopy is essential for resolution of resonan
Three-dimensional solid-state NMR spectroscopy is essential for resolution of resonances from in-plane residues in uniformly (15)N-labeled helical membrane proteins in oriented lipid bilayers.
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Uniformly (15)N-labeled samples of membrane proteins with...
CH-? interaction in VQIVYK sequence elucidated by NMR spectroscopy is essential for PHF formation of tau.
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