Structural highlights
Function
[MVP_MOUSE] Required for normal vault structure. Vaults are multi-subunit structures that may act as scaffolds for proteins involved in signal transduction. Vaults may also play a role in nucleo-cytoplasmic transport. Down-regulates INFG-mediated STAT1 signaling and subsequent activation of JAK. Down-regulates SRC activity and signaling through MAP kinases (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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 A resolution, together with the 2.1-A 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 A model shows major discrepancies, both in the main chain tracing and in the side chain assignment of the two terminal domains R1 and R2.
The mechanism of vault opening from the high resolution structure of the N-terminal repeats of MVP.,Querol-Audi J, Casanas A, Uson I, Luque D, Caston JR, Fita I, Verdaguer N EMBO J. 2009 Nov 4;28(21):3450-7. Epub 2009 Sep 24. PMID:19779459[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Querol-Audi J, Casanas A, Uson I, Luque D, Caston JR, Fita I, Verdaguer N. The mechanism of vault opening from the high resolution structure of the N-terminal repeats of MVP. EMBO J. 2009 Nov 4;28(21):3450-7. Epub 2009 Sep 24. PMID:19779459 doi:10.1038/emboj.2009.274
