{PDOC51224}
{PS51224; MVP}
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* MVP (vault) repeat profile *
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Vaults  are  large  ribonucleoprotein  particles,  composed of three different
proteins  and  one  or  more  small  vault  RNA  (vRNA)  molecules packed into
barrel-shaped  assemblies  that are found in all higher eukaryotes. Their main
component  is  major  vault  protein  (MVP) or lung resistance-related protein
(LRP), which is implicated in resistance to cancer therapy and correlates with
poor prognosis.

The  N-terminal  part  of  MVP  contains  ~8 copies of the vault repeat or MVP
repeat  in  tandem.  The MVP repeat is composed of ~53 amino acids and forms a
structural  part of the vault wall. The C-terminal part of MVP may be involved
in  oligomerization  and be located in the vault cap, while the MVP repeats in
the  N-terminal  part  can be packed like staves in a barrel to form the vault
wall.  The  3D  structure  of the repeat forms a fold that consists of a three
stranded  (B)  antiparallel  beta-sheet  in a unique topology B2-B1-B3 and two
loops  (see  <PDB:1Y7X>). MVP repeats can be interaction-mediating modules, as
MVP repeats 3 and 4 bind vault poly(ADP-ribose) polymerase (VPARP/PARP-4) (see
<PDOC51059>), which is one of the other vault proteins [1].

The profile we developed covers the entire MVP repeat.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: July 2006 / First entry.

[ 1] Kozlov G., Vavelyuk O., Minailiuc O., Banville D., Gehring K.,
     Ekiel I.
     "Solution structure of a two-repeat fragment of major vault protein."
     J. Mol. Biol. 356:444-452(2006).
     PubMed=16373071; DOI=10.1016/j.jmb.2005.11.064

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