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Título

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

Autor Querol-Audí, Jordi ; Casañas, Arnau; Usón, Isabel ; Luque, Daniel; Castón, José R.; Fita, Ignacio ; Verdaguer, Núria
Palabras clave Ribonucleoprotein particle
Signal transduction
Vault
X-ray crystallography
Major vault protein
Fecha de publicación nov-2009
EditorNature Publishing Group
Citación EMBO Journal 28(21): 3450-3457 (2009)
ResumenVaults 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 resolution, together with the 2.1-structure of the seven N-terminal domains (R1-R7) of MVP, reveal the interactions governing vault association and provide an explanation for a reversible dissociation induced by low pH. The structural comparison with the recently published 3.5 model shows major discrepancies, both in the main chain tracing and in the side chain assignment of the two terminal domains R1 and R2. © 2009 European Molecular Biology Organization | All Rights Reserved.
Versión del editorhttp://dx.doi.org/10.1038/emboj.2009.274
URI http://hdl.handle.net/10261/110352
DOI10.1038/emboj.2009.274
Identificadoresdoi: 10.1038/emboj.2009.274
issn: 0261-4189
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