The mechanism of vault opening from the high resolution structure of the N-terminal repeats of MVP

@article{QuerolAudi2009TheMO,
  title={The mechanism of vault opening from the high resolution structure of the N-terminal repeats of MVP},
  author={Jordi Querol-Audí and Arnau Casa{\~n}as and Isabel Us{\'o}n and Daniel Luque and Jos{\'e} R. Cast{\'o}n and Ignasi Fita and N{\'u}ria Verdaguer},
  journal={The EMBO Journal},
  year={2009},
  volume={28},
  pages={3450 - 3457}
}
Vaults are ubiquitous ribonucleoprotein complexes involved in a diversity of cellular processes, including multidrug resistance, transport mechanisms and signal transmission. The vault particle shows a barrel‐shaped structure organized in two identical moieties, each consisting of 39 copies of the major vault protein MVP. Earlier data indicated that vault halves can dissociate at acidic pH. The crystal structure of the vault particle solved at 8 Å resolution, together with the 2.1‐Å structure… 
Structural Dynamics of the Vault Ribonucleoprotein Particle
TLDR
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TLDR
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TLDR
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TLDR
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Direct visualization of vaults within intact cells by electron cryo-tomography
TLDR
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Structure of internalin InlK from the human pathogen Listeria monocytogenes.
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TLDR
The x-ray structure of rat liver vault is determined at 3.5 angstrom resolution and it is shown that the cage structure consists of a dimer of half-vaults, with eachhalf-vault comprising 39 identical major vault protein (MVP) chains.
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TLDR
This study identified and analyzed structural domains involved in vault assembly with emphasis on protein-protein interactions and demonstrated within MVP an intramolecular binding site and show that MVP molecules interact with each other via their coiled coil domain.
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TLDR
EM imaging showed the opening of intact vaults into flowerlike structures when transitioning from neutral to acidic pH, which has potential use in the development of recombinant vault into nanocapsules for drug delivery since one mechanism by which therapeutic agents entrapped in vaults could be released is through an opening of the intact vault structure.
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TLDR
These particles are the first example of a single protein polymerizing into a non-spherically, non-cylindrically symmetrical structure and will enable us to design agents that disrupt vault formation and aid in elucidating vault functionin vivo.
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TLDR
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TLDR
A structural model is proposed that predicts the stoichiometry of vault proteins and RNA, defines vault dimer-monomer interactions, and describes two possible modes for unfolding of vaults into flowers, likely to play a role in vault function.
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