Study of Conformational and Dynamic Changes upon
Phosphorylation of Proline Rich Region of Tau210-240 Peptide
Using Molecular Dynamic Simulation

a 2021

Study of Conformational and Dynamic Changes upon Phosphorylation of Proline Rich Region of Tau210-240 Peptide Using Molecular Dynamic Simulation

BERA, Krishnendu, A. LASORSA, I. MALKI, E. DUPRE, F.X. CANTRELLE et. al.

Základní údaje

Originální název

Study of Conformational and Dynamic Changes upon Phosphorylation of Proline Rich Region of Tau210-240 Peptide Using Molecular Dynamic Simulation

Autoři

BERA, Krishnendu (356 Indie, domácí), A. LASORSA, I. MALKI, E. DUPRE, F.X. CANTRELLE, H. MERZOUGUI, D. SINNAEVE, X. HANOULLE, Jozef HRITZ (703 Slovensko, domácí) a I. LANDRIEU

Vydání

2021

Další údaje

Jazyk

angličtina

Typ výsledku

Konferenční abstrakt

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Česká republika

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Kód RIV

RIV/00216224:14740/21:00121211

Organizační jednotka

Středoevropský technologický institut

Klíčová slova anglicky

Molecular Dynamic Simulation; Tau210-240

Štítky

rivok

Změněno: 10. 3. 2021 15:12, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

The conformational and dynamic changes of protein interaction regulated by posttranslational modifications such as phosphorylation of intrinsically disordered proteins (IDPs), remains challenging to elucidate. Tau, which is a well-known IDP and its phosphorylation is of particular interest because Tau is found hyperthe conformational and dynamic changes upon phosphorylation of Tau. The proline-rich motif recognized within Tau210-240 peptide directly interact with AD progression protein such as 14-3-3. Microsecond time scale molecular dynamic simulation studies performed for apo and phosphorylated residues (212PThr, 217PThr, 231PThr, 235PSer) Tau peptide210-240 using three different temperature variants (278° K, 298° K and 310° K) and two different force field parameters (AMBER99SB-ILDN and CHARMM36m) with TIP4PD water model. These four-phosphorylation causing increase in compactness. The strong salt bridges are forming with nearby lysine and arginine due to the phosphorylation, which may alter the binding of associated protein like 14-3-3 with Tau. Phosphorylation induces a strong structural transition, with Tau210 240 favouring a bent conformation. The MD simulation results were verified using NMR experimental parameters like chemical shift, 3J-coupling etc. The experimental part has been carried out by our collaborator Prof. Isabelle Landrieu.

Návaznosti

LTAUSA18168, projekt VaV

Název: Selektivní NMR značení jako nástroj pro charakterizaci proteinových komplexů zapojených do neurodegenerativních onemocnění

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Selektivní NMR značení jako nástroj pro charakterizaci proteinových komplexů zapojených do neurodegenerativních onemocnění, INTER-ACTION

Citovat

BERA, Krishnendu, A. LASORSA, I. MALKI, E. DUPRE, F.X. CANTRELLE, H. MERZOUGUI, D. SINNAEVE, X. HANOULLE, Jozef HRITZ a I. LANDRIEU. Study of Conformational and Dynamic Changes upon Phosphorylation of Proline Rich Region of Tau210-240 Peptide Using Molecular Dynamic Simulation. 2021.

@proceedings{1751020,
   author = {Bera, Krishnendu and Lasorsa, A. and Malki, I. and Dupre, E. and Cantrelle, F.X. and Merzougui, H. and Sinnaeve, D. and Hanoulle, X. and Hritz, Jozef and Landrieu, I.},
   keywords = {Molecular Dynamic Simulation; Tau210-240},
   language = {eng},
   title = {Study of Conformational and Dynamic Changes upon Phosphorylation of Proline Rich Region of Tau210-240 Peptide Using Molecular Dynamic Simulation},
   url = {https://www.ceitec.eu/abstract-book-2021-final-pdf/f43850},
   year = {2021}
}

TY  - CONF
ID  - 1751020
AU  - Bera, Krishnendu - Lasorsa, A. - Malki, I. - Dupre, E. - Cantrelle, F.X. - Merzougui, H. - Sinnaeve, D. - Hanoulle, X. - Hritz, Jozef - Landrieu, I.
PY  - 2021
TI  - Study of Conformational and Dynamic Changes upon Phosphorylation of Proline Rich Region of Tau210-240 Peptide Using Molecular Dynamic Simulation
KW  - Molecular Dynamic Simulation
KW  - Tau210-240
UR  - https://www.ceitec.eu/abstract-book-2021-final-pdf/f43850
N2  - The conformational and dynamic changes of protein interaction regulated by posttranslational modifications such as phosphorylation of intrinsically disordered proteins (IDPs), remains challenging to elucidate. Tau, which is a well-known IDP and its phosphorylation is of particular interest because Tau is found hyperthe conformational and dynamic changes upon phosphorylation of Tau. The proline-rich motif recognized within Tau210-240 peptide directly interact with AD progression protein such as 14-3-3. Microsecond time scale molecular dynamic simulation studies performed for apo and phosphorylated residues (212PThr, 217PThr, 231PThr, 235PSer) Tau peptide210-240 using three different temperature variants (278° K, 298° K and 310° K) and two different force field parameters (AMBER99SB-ILDN and CHARMM36m) with TIP4PD water model. These four-phosphorylation causing increase in compactness. The strong salt bridges are forming with nearby lysine and arginine due to the phosphorylation, which may alter the binding of associated protein like 14-3-3 with Tau. Phosphorylation induces a strong structural transition, with Tau210 240 favouring a bent conformation. The MD simulation results were verified using NMR experimental parameters like chemical shift, 3J-coupling etc. The experimental part has been carried out by our collaborator Prof. Isabelle Landrieu.
ER  -

BERA, Krishnendu, A. LASORSA, I. MALKI, E. DUPRE, F.X. CANTRELLE, H. MERZOUGUI, D. SINNAEVE, X. HANOULLE, Jozef HRITZ a I. LANDRIEU. \textit{Study of Conformational and Dynamic Changes upon Phosphorylation of Proline Rich Region of Tau210-240 Peptide Using Molecular Dynamic Simulation}. 2021.

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