Oligomerization of a Retroviral Matrix Protein Is Facilitated by Backbone Flexibility on Nanosecond Time Scale
The result's identifiers
Result code in 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>
Alternative codes found
RIV/60461373:22330/11:43877186 RIV/60461373:22810/11:43877186
Result on the web
<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>
Alternative languages
Result language
angličtina
Original language name
Oligomerization of a Retroviral Matrix Protein Is Facilitated by Backbone Flexibility on Nanosecond Time Scale
Original language description
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
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
BO - Biophysics
OECD FORD branch
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Result continuities
Project
<a href="/en/project/GA203%2F07%2F0872" target="_blank" >GA203/07/0872: Functional and structural study of mutants of matrix protein from Mason-Pfizer monkey virus which affects budding</a><br>
Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach
Others
Publication year
2011
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Physical Chemistry B
ISSN
1520-6106
e-ISSN
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Volume of the periodical
2011
Issue of the periodical within the volume
115
Country of publishing house
US - UNITED STATES
Number of pages
11
Pages from-to
2634-2644
UT code for WoS article
000288401100018
EID of the result in the Scopus database
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