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Structural dynamics of the vault ribonucleoprotein particle

AutorCasañas, Arnau; Querol-Audí, Jordi ; Fita, Ignacio ; Verdaguer, Núria
Fecha de publicación2012
CitaciónMacromolecular Crystallography: 173-182 (2012)
SerieNATO Science for Peace and Security Series A: Chemistry and Biology 2012
ResumenVaults are ubiquitous, highly conserved, 13 MDa ribonucleoprotein particles, involved in a diversity of cellular processes, including multidrug resistance, transport mechanisms and signal transmission. There are between 10 4 and 10 6 vault particles per mammalian cell and they do not trigger autoimmunity. The vault particle shows a hollow barrel-shaped structure organized in two identical moieties, each consisting of 39 copies of the major vault protein (MVP). Other data indicated that vault halves can dissociate at acidic pH. The high resolution, crystal structure of the of the seven N-terminal domains (R1-R7) of MVP, forming the central vault barrel, together with that of the native vault particle (solved at 8 Å resolution), revealed the interactions governing vault association and suggested a pH-dependent mechanism for a reversible dissociation induced by low pH. Vault particles posses many features making them very promising vehicles for the delivery of therapeutic agents including self-assembly, 100 nm size range, emerging atomic-level structural information, natural presence in humans ensuring biocompability, recombinant production system, existing features for targeting species to the large lumen and a dynamic structure that may be controlled for manipulation of drug release kinetics. All these attributes provide vaults with enormous potential as a drug/gene delivery platform. © 2012 Springer Science+Business Media B.V.
Identificadoresdoi: 10.1007/978-94-007-2530-0_16
isbn: 978-94-007-2529-4
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