Structural view of the Ran-Importin beta interaction at 2.3 A resolution.
Structural view of the Ran-Importin beta interaction at 2.3 A resolution.
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发表时间：
1999
期刊：
影响因子：
64.5
通讯作者：
I. Vetter;A. Arndt;U. Kutay;D. Görlich;A. Wittinghofer
中科院分区：
文献类型：
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作者：
I. Vetter;A. Arndt;U. Kutay;D. Görlich;A. Wittinghofer
输入蛋白家族的转运受体在细胞核和细胞质之间穿梭，并通过核孔复合物介导大分子的转运。它们与gtp结合蛋白Ran特异性地相互作用，后者反过来调节它们与货物的相互作用。在这里，我们报道了Ran与不可水解的GTP类似物GppNHp结合的复合物的三维结构和来自Importin β的462残基片段。Importin β的结构有10个类似HEAT和Armadillo基序的串联重复序列。它们形成不规则的新月形，其凹处形成与ran -三磷酸的界面。Ran的进口蛋白结合位点与RanBP2的Ran结合域不重叠。
Transport receptors of the Importin beta family shuttle between the nucleus and cytoplasm and mediate transport of macromolecules through nuclear pore complexes. They interact specifically with the GTP-binding protein Ran, which in turn regulates their interaction with cargo. Here, we report the three-dimensional structure of a complex between Ran bound to the nonhydrolyzable GTP analog GppNHp and a 462-residue fragment from Importin beta. The structure of Importin beta shows 10 tandem repeats resembling HEAT and Armadillo motifs. They form an irregular crescent, the concave site of which forms the interface with Ran-triphosphate. The importin-binding site of Ran does not overlap with that of the Ran-binding domain of RanBP2.