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Statements

Subject Item
n2:RIV%2F60461373%3A22810%2F11%3A43877186%21RIV12-MSM-22810___
rdf:type
skos:Concept n12:Vysledek
dcterms: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 molecular dynamics 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 α-helices α2 and α3 and the C-terminal half of α-helix α3 which accommodate amino 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 document that conformational selection mechanism together with induced fit and favorable structural preorganization play an important role in the control of the oligomerization process. 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 molecular dynamics 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 α-helices α2 and α3 and the C-terminal half of α-helix α3 which accommodate amino 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 document that conformational selection mechanism together with induced fit and favorable structural preorganization play an important role in the control of the oligomerization process.
dcterms:title
Oligomerization of a Retroviral Matrix Protein Is Facilitated by Backbone Flexibility on Nanosecond Time Scale Oligomerization of a Retroviral Matrix Protein Is Facilitated by Backbone Flexibility on Nanosecond Time Scale
skos:prefLabel
Oligomerization of a Retroviral Matrix Protein Is Facilitated by Backbone Flexibility on Nanosecond Time Scale Oligomerization of a Retroviral Matrix Protein Is Facilitated by Backbone Flexibility on Nanosecond Time Scale
skos:notation
RIV/60461373:22810/11:43877186!RIV12-MSM-22810___
n12:predkladatel
n13:orjk%3A22810
n3:aktivita
n7:Z n7:S n7:P
n3:aktivity
P(GA203/07/0872), S, Z(MSM0021620835)
n3:cisloPeriodika
11
n3:dodaniDat
n11:2012
n3:domaciTvurceVysledku
n16:1891928 n16:4866754 n16:8470200
n3:druhVysledku
n19:J
n3:duvernostUdaju
n4:S
n3:entitaPredkladatele
n8:predkladatel
n3:idSjednocenehoVysledku
217888
n3:idVysledku
RIV/60461373:22810/11:43877186
n3:jazykVysledku
n18:eng
n3:klicovaSlova
conformational selection; oligomerization; matrix protein; Mason-Pfizer monkey virus
n3:klicoveSlovo
n14:matrix%20protein n14:Mason-Pfizer%20monkey%20virus n14:oligomerization n14:conformational%20selection
n3:kodStatuVydavatele
US - Spojené státy americké
n3:kontrolniKodProRIV
[BED04AB83053]
n3:nazevZdroje
JOURNAL OF PHYSICAL CHEMISTRY B
n3:obor
n10:BO
n3:pocetDomacichTvurcuVysledku
3
n3:pocetTvurcuVysledku
7
n3:projekt
n20:GA203%2F07%2F0872
n3:rokUplatneniVysledku
n11:2011
n3:svazekPeriodika
115
n3:tvurceVysledku
Hrabal, Richard Srb, Pavel Lang, Jan Ruml, Tomáš Grocký, Marián Vlach, Jiří Prchal, Jan
n3:wos
000288401100018
n3:zamer
n5:MSM0021620835
s:issn
1520-6106
s:numberOfPages
11
n15:organizacniJednotka
22810