1y7x

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Solution structure of a two-repeat fragment of major vault protein

Structural highlights

1y7x is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MVP_HUMAN 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.[1] [2] [3]

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

Major vault protein (MVP) is the main constituent of vaults, large ribonucleoprotein particles implicated in resistance to cancer therapy and correlated with poor survival prognosis. Here, we report the structure of the main repeat element in human MVP. The approximately 55 amino acid residue MVP domain has a unique, novel fold that consists of a three-stranded antiparallel beta-sheet. The solution NMR structure of a two-domain fragment reveals the interdomain contacts and relative orientations of the two MVP domains. We use these results to model the assembly of 672 MVP domains from 96 MVP molecules into the ribs of the 13MDa vault structure. The unique features include a thin, skin-like structure with polar residues on both the cytoplasmic and internal surface, and a pole-to-pole arrangement of MVP molecules. These studies provide a starting point for understanding the self-assembly of MVP into vaults and their interactions with other proteins. Chemical shift perturbation studies identified the binding site of vault poly(ADP-ribose) polymerase, another component of vault particles, indicating that MVP domains form a new class of interaction-mediating modules.

Solution structure of a two-repeat fragment of major vault protein.,Kozlov G, Vavelyuk O, Minailiuc O, Banville D, Gehring K, Ekiel I J Mol Biol. 2006 Feb 17;356(2):444-52. Epub 2005 Dec 7. PMID:16373071[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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References

  1. ↑ Kolli S, Zito CI, Mossink MH, Wiemer EA, Bennett AM. The major vault protein is a novel substrate for the tyrosine phosphatase SHP-2 and scaffold protein in epidermal growth factor signaling. J Biol Chem. 2004 Jul 9;279(28):29374-85. Epub 2004 May 7. PMID:15133037 doi:http://dx.doi.org/10.1074/jbc.M313955200
  2. ↑ Kim E, Lee S, Mian MF, Yun SU, Song M, Yi KS, Ryu SH, Suh PG. Crosstalk between Src and major vault protein in epidermal growth factor-dependent cell signalling. FEBS J. 2006 Feb;273(4):793-804. PMID:16441665 doi:http://dx.doi.org/10.1111/j.1742-4658.2006.05112.x
  3. ↑ Steiner E, Holzmann K, Pirker C, Elbling L, Micksche M, Sutterluty H, Berger W. The major vault protein is responsive to and interferes with interferon-gamma-mediated STAT1 signals. J Cell Sci. 2006 Feb 1;119(Pt 3):459-69. Epub 2006 Jan 17. PMID:16418217 doi:http://dx.doi.org/10.1242/jcs.02773
  4. ↑ 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. 2006 Feb 17;356(2):444-52. Epub 2005 Dec 7. PMID:16373071 doi:10.1016/j.jmb.2005.11.064

Contents


PDB ID 1y7x

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OCA

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