The Structure of Rat Liver Vault at 3.5 Angstrom Resolution
The Structure of Rat Liver Vault at 3.5 Angstrom Resolution
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DOI：
10.1126/science.1164975
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发表时间：
2009-01-16
期刊：
影响因子：
56.9
通讯作者：
Tsukihara, Tomitake
中科院分区：
文献类型：
--
作者：
Tanaka, Hideaki;Kato, Koji;Tsukihara, Tomitake
穹窿是最大的细胞质核糖核蛋白颗粒之一，存在于许多真核生物中。人们已经提出了在多药耐药性和先天免疫中的作用，但细胞功能仍不清楚。我们已经确定了大鼠肝穹窿在3.5埃分辨率的X射线结构，并表明笼状结构由半穹窿的二聚体组成，每个半穹窿包含39个相同的主要穹窿蛋白（MVP）链。每个MVP单体折叠成12个结构域：9个结构重复结构域、一个肩结构域、一个帽-螺旋结构域和一个帽-环结构域。42圈长的帽-螺旋结构域之间的相互作用是稳定颗粒的关键。肩部结构域在结构上类似于气孔蛋白的核心结构域，气孔蛋白是红细胞和上皮细胞中的脂筏组分。
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.