Nonmyristoylated Matrix Protein from the Mason-Pfizer Monkey Virus Forms Oligomers

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11320%2F09%3A00207054" target="_blank" >RIV/00216208:11320/09:00207054 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60461373:22810/09:00022561

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Nonmyristoylated Matrix Protein from the Mason-Pfizer Monkey Virus Forms Oligomers

Popis výsledku v původním jazyce

We studied oligomeric properties of betaretroviral Mason-Pfizer monkey virus (M-PMV) non-myristoylated matrix protein (MA) and its R55F mutant in solution by means of nuclear magnetic resonance (NMR) spectroscopy. Using concentration-dependent NMR chemical shift mapping we have proven that the wild type (WT) MA forms oligomers in solution. Conversely, no oligomerization was observed for the R55F mutant. Structural comparison of matrix proteins explains their different behavior in solution, concluding that the key residues involved in the intermonomeric interaction residues are exposed in WT MA while being buried in the mutant, which prevents the oligomerization of R55F. The final model of oligomerization of wt MA was derived by a novel method of concerted use of the chemical shifts mapping and diffusion-ordered spectroscopy (DOSY) measured on a set of protein samples with varying concentrations.

Název v anglickém jazyce

Nonmyristoylated Matrix Protein from the Mason-Pfizer Monkey Virus Forms Oligomers

Popis výsledku anglicky

We studied oligomeric properties of betaretroviral Mason-Pfizer monkey virus (M-PMV) non-myristoylated matrix protein (MA) and its R55F mutant in solution by means of nuclear magnetic resonance (NMR) spectroscopy. Using concentration-dependent NMR chemical shift mapping we have proven that the wild type (WT) MA forms oligomers in solution. Conversely, no oligomerization was observed for the R55F mutant. Structural comparison of matrix proteins explains their different behavior in solution, concluding that the key residues involved in the intermonomeric interaction residues are exposed in WT MA while being buried in the mutant, which prevents the oligomerization of R55F. The final model of oligomerization of wt MA was derived by a novel method of concerted use of the chemical shifts mapping and diffusion-ordered spectroscopy (DOSY) measured on a set of protein samples with varying concentrations.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

BO - Biofyzika

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2009

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Molecular Biology

ISSN

0022-2836

e-ISSN

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Svazek periodika

390

Číslo periodika v rámci svazku

5

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

14

Strana od-do

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Kód UT WoS článku

000268556400011

EID výsledku v databázi Scopus

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