Structural studies of large nucleoprotein particles, vaults.
Structural studies of large nucleoprotein particles, vaults.
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DOI:
10.2183/pjab.88.416
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发表时间:
2012
期刊:
影响因子:
--
通讯作者:
Tsukihara T
中科院分区:
文献类型:
--
作者:
Tanaka H;Tsukihara T
Vault is the largest nonicosahedral cytosolic nucleoprotein particle ever described. The widespread presence and evolutionary conservation of vaults suggest important biologic roles, although their functions have not been fully elucidated. X-ray structure of vault from rat liver was determined at 3.5 Å resolution. It exhibits an ovoid shape with a size of 40 × 40 × 67 nm3. The cage structure of vault 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 other components of vaults, telomerase-associated proteins, poly(ADP-ribose) polymerases and small RNAs, are in location in the vault particle by electron microscopy.
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影响因子:
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作者:
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通讯作者:
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DOI:
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发表时间:
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期刊:
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影响因子:
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通讯作者:
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影响因子:
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