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

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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. (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/riv/aktivita
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
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 217888
http://linked.open...ai/riv/idVysledku
  • RIV/60461373:22810/11:43877186
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • conformational selection; oligomerization; matrix protein; Mason-Pfizer monkey virus (en)
http://linked.open.../riv/klicoveSlovo
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
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
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
issn
  • 1520-6106
number of pages
http://localhost/t...ganizacniJednotka
  • 22810
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