The structure of the scaffold nucleoporin Nup120 reveals a new and unexpected domain architecture.

The structure of the scaffold nucleoporin Nup120 reveals a new and unexpected domain architecture.
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DOI:
10.1016/j.str.2009.06.003
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发表时间:
2009-08-12
期刊:
Structure (London, England : 1993)
影响因子:
--
通讯作者:
Schwartz TU
Schwartz TU
中科院分区:
其他
文献类型:
--
作者:
Leksa NC;Brohawn SG;Schwartz TU

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核质运输是由核孔复合体(NPC)介导的,核孔复合体是位于核膜圆形开口中的巨大蛋白质集合。NPC是模块化的,具有暂态和稳定的组件。稳定的核心基本上是由两个多蛋白复合体组成的,Y形七聚体Nup84复合体和Nic96复合体围绕八个轴排列。我们给出了Nup1201-757的晶体结构,它是Y型Nup84络合物的两个短臂之一。该蛋白质采用紧凑的椭圆形,围绕着一个新的两部分α-螺旋结构域与β-螺旋体结构域紧密结合。结构域的排列与形成Y的另一短臂的Nup85·Seh1复合体有很大不同。根据这里提供的数据,我们确定了Y型Nup84复合体的所有三个分支都通过螺旋相互作用紧密相连,β-螺旋桨可能从相互作用部位(S)到邻近的复合体。
Nucleocytoplasmic transport is mediated by nuclear pore complexes (NPCs), enormous protein assemblies residing in circular openings in the nuclear envelope. The NPC is modular, with transient and stable components. The stable core is essentially built from two multiprotein complexes, the Y-shaped heptameric Nup84 complex and the Nic96 complex, arranged around an eightfold axis. We present the crystal structure of Nup1201-757, one of the two short arms of the Y-shaped Nup84 complex. The protein adopts a compact oval shape built around a novel bipartite α-helical domain intimately integrated with a β-propeller domain. The domain arrangement is substantially different from the Nup85•Seh1 complex, which forms the other short arm of the Y. With the data presented here we establish that all three branches of the Y-shaped Nup84 complex are tightly connected by helical interactions and that the β-propellers likely form interaction site(s) to neighboring complexes.
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影响因子: 2.2
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