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TitleThe structure of rat liver vault at 3.5 angstrom resolution
Journal, issue, pagesScience, Vol. 323, Page 384-388, Year 2009
Publish dateOct 24, 2008 (structure data deposition date)
AuthorsHideaki Tanaka / Koji Kato / Eiki Yamashita / Tomoyuki Sumizawa / Yong Zhou / Min Yao / Kenji Iwasaki / Masato Yoshimura / Tomitake Tsukihara /
PubMed AbstractVaults are among the largest cytoplasmic ribonucleoprotein particles and are found in numerous eukaryotic species. Roles in multidrug resistance and innate immunity have been suggested, but the ...Vaults are among the largest cytoplasmic ribonucleoprotein particles and are found in numerous eukaryotic species. Roles in multidrug resistance and innate immunity have been suggested, but the cellular function remains unclear. We have determined the x-ray structure of rat liver vault at 3.5 angstrom resolution and show that the cage structure consists of a dimer of half-vaults, with each half-vault comprising 39 identical major vault protein (MVP) chains. Each MVP monomer folds into 12 domains: nine structural repeat domains, a shoulder domain, a cap-helix domain, and a cap-ring domain. Interactions between the 42-turn-long cap-helix domains are key to stabilizing the particle. The shoulder domain is structurally similar to a core domain of stomatin, a lipid-raft component in erythrocytes and epithelial cells.
External linksScience / PubMed:19150846
MethodsX-ray diffraction
Resolution3.5 Å
Structure data

PDB-4v60:
The structure of rat liver vault at 3.5 angstrom resolution
Method: X-RAY DIFFRACTION / Resolution: 3.5 Å

Source
  • rattus norvegicus (Norway rat)
KeywordsSTRUCTURAL PROTEIN / 9 REPEAT DOMAINS / PROTEIN-PROTEIN COMPLEX / Ribonucleoprotein

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