The structure of rat liver vault at 3.5 angstrom resolution

Hideaki Tanaka, Koji Kato, Eiki Yamashita, Tomoyuki Sumizawa, Yong Zhou, Min Yao, Kenji Iwasaki, Masato Yoshimura, Tomitake Tsukihara

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119 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)384-388
Number of pages5
Issue number5912
Publication statusPublished - Jan 16 2009
Externally publishedYes

ASJC Scopus subject areas

  • General


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