Nuclear Magnetic Resonance Spectroscopy Insights into Tau Structure in Solution: Impact of Post-translational Modifications
| Autor: | Alessia Lasorsa, Xavier Hanoulle, Elian Dupre, Caroline Smet-Nocca, Clément Danis, João Filipe Neves, Isabelle Landrieu, Robert Schneider |
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| Přispěvatelé: | Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Université de Lille-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
Tau protein
tau Proteins Isomerase Protein Structure Secondary 03 medical and health sciences 0302 clinical medicine Humans Peptide bond [CHIM]Chemical Sciences [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology 030212 general & internal medicine Phosphorylation [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM] Spectroscopy Nuclear Magnetic Resonance Biomolecular ComputingMilieux_MISCELLANEOUS Quantitative Biology::Biomolecules biology Chemistry Trans conformation Nuclear magnetic resonance spectroscopy [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM] Tau phosphorylation Posttranslational modification Biophysics biology.protein Protein Processing Post-Translational |
| Zdroj: | Advanced in Experimental Medical Biology Advanced in Experimental Medical Biology, pp.35-45, 2019, ⟨10.1007/978-981-32-9358-8_3⟩ Advances in Experimental Medicine and Biology Advances in Experimental Medicine and Biology-Tau Biology Advances in Experimental Medicine and Biology ISBN: 9789813293571 Tau Biology |
| ISSN: | 0065-2598 2214-8019 |
| Popis: | Although Tau is an intrinsically disordered protein, some level of structure can still be defined, corresponding to short stretches of dynamic secondary structures and a preferential global fold described as an ensemble of conformations. These structures can be modified by Tau phosphorylation, and potentially other post-translational modifications. The analytical capacity of Nuclear Magnetic Resonance (NMR) spectroscopy provides the advantage of offering a residue-specific view of these modifications, allowing to link specific sites to a particular structure. The cis or trans conformation of X-Proline peptide bonds is an additional characteristic parameter of Tau structure that is targeted and modified by prolyl cis/trans isomerases. The challenge in molecular characterization of Tau lies in being able to link structural parameters to functional consequences in normal functions and dysfunctions of Tau, including potential misfolding on the path to aggregation and/or perturbation of the interactions of Tau with its many molecular partners. Phosphorylation of Ser and Thr residues has the potential to impact the local and global structure of Tau. |
| Databáze: | OpenAIRE |
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