Oligomerization of a Retroviral Matrix Protein Is Facilitated by Backbone Flexibility on Nanosecond Time Scale
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11320%2F11%3A10107502" target="_blank" >RIV/00216208:11320/11:10107502 - isvavai.cz</a>
Nalezeny alternativní kódy
RIV/60461373:22330/11:43877186 RIV/60461373:22810/11:43877186
Výsledek na webu
<a href="http://dx.doi.org/10.1021/jp110420m" target="_blank" >http://dx.doi.org/10.1021/jp110420m</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/jp110420m" target="_blank" >10.1021/jp110420m</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Oligomerization of a Retroviral Matrix Protein Is Facilitated by Backbone Flexibility on Nanosecond Time Scale
Popis výsledku v původním jazyce
The oligomerization capacity of the retroviral matrix protein is an important feature that affects assembly of immature virions and their interaction with cellular membrane. A combination of NMR relaxation measurements and advanced analysis of moleculardynamics simulation trajectory provided an unprecedentedly detailed insight into internal mobility of matrix proteins of the Mason-Pfizer monkey virus. Strong evidence have been obtained that the oligomerization capacity of the wild-type matrix protein is closely related to the enhanced dynamics of several parts of its backbone on a nanosecond time scale. Increased flexibility has been observed for two regions: the loop between R-helices R2 and R3 and the C-terminal half of R-helix R3 which accommodateamino acid residues that form the oligomerization interface. On the other hand, matrix mutant R55F that has changed structure and does not exhibit any specific oligomerization in solution was found considerably more rigid. Our results doc
Název v anglickém jazyce
Oligomerization of a Retroviral Matrix Protein Is Facilitated by Backbone Flexibility on Nanosecond Time Scale
Popis výsledku anglicky
The oligomerization capacity of the retroviral matrix protein is an important feature that affects assembly of immature virions and their interaction with cellular membrane. A combination of NMR relaxation measurements and advanced analysis of moleculardynamics simulation trajectory provided an unprecedentedly detailed insight into internal mobility of matrix proteins of the Mason-Pfizer monkey virus. Strong evidence have been obtained that the oligomerization capacity of the wild-type matrix protein is closely related to the enhanced dynamics of several parts of its backbone on a nanosecond time scale. Increased flexibility has been observed for two regions: the loop between R-helices R2 and R3 and the C-terminal half of R-helix R3 which accommodateamino acid residues that form the oligomerization interface. On the other hand, matrix mutant R55F that has changed structure and does not exhibit any specific oligomerization in solution was found considerably more rigid. Our results doc
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
BO - Biofyzika
OECD FORD obor
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Návaznosti výsledku
Projekt
<a href="/cs/project/GA203%2F07%2F0872" target="_blank" >GA203/07/0872: Funkční a strukturní studie mutantů matrixového proteinu Mason-Pfizerova opičího viru ovlivňující jeho uvolnění z buňky</a><br>
Návaznosti
Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach
Ostatní
Rok uplatnění
2011
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Journal of Physical Chemistry B
ISSN
1520-6106
e-ISSN
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Svazek periodika
2011
Číslo periodika v rámci svazku
115
Stát vydavatele periodika
US - Spojené státy americké
Počet stran výsledku
11
Strana od-do
2634-2644
Kód UT WoS článku
000288401100018
EID výsledku v databázi Scopus
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