Structural view of the Ran-importin β interaction at 2.3 Å resolution

被引：291
作者：
Vetter, IR
Arndt, A
Kutay, U
Görlich, D
Wittinghofer, A
机构：
[1] Max Planck Inst Mol Physiol, D-44227 Dortmund, Germany
[2] Heidelberg Univ, Zentrum Mol Biol, D-69120 Heidelberg, Germany
来源：
CELL | 1999年 / 97卷 / 05期
关键词：
D O I：
10.1016/S0092-8674(00)80774-6
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
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收藏
页码：635 / 646
页数：12
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