Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1
Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1
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DOI：
10.1038/nsb773
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发表时间：
2002-04-01
期刊：
影响因子：
--
通讯作者：
Stewart, M
中科院分区：
文献类型：
--
作者：
Grant, RP;Hurt, E;Stewart, M
脊椎动物Tap蛋白是用于mRNA核输出的穿梭转运受体NXF家族的成员。TAP具有模块化结构，其最C-末端结构域对于与含有FG重复的核孔蛋白（FG-核孔蛋白）结合是重要的，并且足以介导核穿梭。我们报告的解决方案结构的C-末端结构域，这是基于一个独特的安排，四个α-螺旋，并加入到下一个模块由一个灵活的12个残基Pro丰富的接头。F617 A Tap通过最C-末端结构域抑制FG-核孔蛋白结合，该结构域与构建Tap的其他模块的结构一起为其核穿梭功能提供结构背景。
The vertebrate Tap protein is a member of the NXF family of shuttling transport receptors for nuclear export of mRNA. Tap has a modular structure, and its most C-terminal domain is important for binding to FG repeat-containing nuclear pore proteins (FG-nucleoporins) and is sufficient to mediate nuclear shuttling. We report the solution structure of this C-terminal domain, which is based on a distinctive arrangement of four alpha-helices and is joined to the next module by a flexible 12-residue Pro-rich linker. F617A Tap suppresses FG-nucleoporin binding by the most C-terminal domain that, together with the structure of the other modules from which Tap is constructed, provides a structural context for its nuclear shuttling function.