Journal
SCIENCE
Volume 323, Issue 5912, Pages 384-388Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1164975
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Funding
- Ministry of Education, Culture, Sports, Science, and Technology of Japan [10188101, 10179101, A-041, 19770082, 16048216, 20051001]
- Japan Space Forum
- Grants-in-Aid for Scientific Research [16048216, 10188101, 19770082, 10179101] Funding Source: KAKEN
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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.
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