About: Oligomerization of a Retroviral Matrix Protein Is Facilitated by Backbone Flexibility on Nanosecond Time Scale

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
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&#8722;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 &#945;-helices &#945;2 and &#945;3 and the C-terminal half of &#945;-helix &#945;3 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&#8722;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 &#945;-helices &#945;2 and &#945;3 and the C-terminal half of &#945;-helix &#945;3 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. (en)
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 (en)
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 (en)
skos:notation	RIV/60461373:22810/11:43877186!RIV12-MSM-22810___
http://linked.open...avai/predkladatel	Rektorát
http://linked.open...avai/riv/aktivita	P S Z
http://linked.open...avai/riv/aktivity	P(GA203/07/0872), S, Z(MSM0021620835)
http://linked.open...iv/cisloPeriodika	11
http://linked.open...vai/riv/dodaniDat	2012
http://linked.open...aciTvurceVysledku	Lang, Jan Hrabal, Richard Srb, Pavel
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Vysoká škola chemicko-technologická v Praze / Rektorát
http://linked.open...dnocenehoVysledku	217888
http://linked.open...ai/riv/idVysledku	RIV/60461373:22810/11:43877186
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	conformational selection; oligomerization; matrix protein; Mason-Pfizer monkey virus (en)
http://linked.open.../riv/klicoveSlovo	Mason-Pfizer monkey virus conformational selection matrix protein oligomerization
http://linked.open...odStatuVydavatele	US - Spojené státy americké
http://linked.open...ontrolniKodProRIV	[BED04AB83053]
http://linked.open...i/riv/nazevZdroje	JOURNAL OF PHYSICAL CHEMISTRY B
http://linked.open...in/vavai/riv/obor	BO
http://linked.open...ichTvurcuVysledku	3 (xsd:int)
http://linked.open...cetTvurcuVysledku	7 (xsd:int)
http://linked.open...vavai/riv/projekt	Functional and structural study of mutants of matrix protein from Mason-Pfizer monkey virus which affects budding
http://linked.open...UplatneniVysledku	2011
http://linked.open...v/svazekPeriodika	115
http://linked.open...iv/tvurceVysledku	Vlach, Jiří Hrabal, Richard Lang, Jan Prchal, Jan Ruml, Tomáš Srb, Pavel Grocký, Marián
http://linked.open...ain/vavai/riv/wos	000288401100018
http://linked.open...n/vavai/riv/zamer	Fyzika molekulárních, makromolekulárních a biologických systémů
issn	1520-6106
number of pages	11 (xsd:int)
http://localhost/t...ganizacniJednotka	22810
is http://linked.open...avai/riv/vysledek of	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

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