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首页> 外文期刊>Journal of Molecular Biology >The adoption of a twisted structure of importin-beta is essential for the protein-protein interaction required for nuclear transport.
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The adoption of a twisted structure of importin-beta is essential for the protein-protein interaction required for nuclear transport.

机译：importin-beta的扭曲结构的采用对于核转运所需的蛋白质-蛋白质相互作用至关重要。

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摘要

Importin-beta is a nuclear transport factor which mediates the nuclear import of various nuclear proteins. The N-terminal 1-449 residue fragment of mouse importin-beta (impbeta449) possesses the ability to bidirectionally translocate through the nuclear pore complex (NPC), and to bind RanGTP. The structure of the uncomplexed form of impbeta449 has been solved at a 2.6 A resolution by X-ray crystallography. It consists of ten copies of the tandemly arrayed HEAT repeat and exhibits conformational flexibility which is involved in protein-protein interaction for nuclear transport. The overall conformation of the HEAT repeats shows that a twisted motion produces a significantly varied superhelical architecture from the previously reported structure of RanGTP-bound importin-beta. These conformational changes appear to be the sum of small conformational changes throughout the polypeptide. Such a flexibility, which resides in the stacked HEAT repeats, is essential for interaction with RanGTP or with NPCs. Furthermore, it was found that impbeta449 has a structural similarity with another nuclear migrating protein, namely beta-catenin, which is composed of another type of helix-repeated structure of ARM repeat. Interestingly, the essential regions for NPC translocation for both importin-beta and beta-catenin are spatially well overlapped with one another. This strongly indicates the importance of helix stacking of the HEAT or ARM repeats for NPC-passage. Copyright 2000 Academic Press.
机译：Importin-beta是一种核转运因子，可介导各种核蛋白的核输入。小鼠importin-beta（impbeta449）的N端1-449残基片段具有双向移位通过核孔复合物（NPC）的能力，并能结合RanGTP。 X射线晶体学已以2.6 A的分辨率解决了impbeta449非复杂形式的结构。它由十个串联排列的HEAT重复序列组成，并具有构象柔韧性，涉及核转运蛋白与蛋白的相互作用。 HEAT重复序列的整体构象表明，扭转运动会产生与以前报道的RanGTP结合的importin-beta结构显着不同的超螺旋结构。这些构象变化似乎是整个多肽中小的构象变化的总和。这种灵活性（位于堆叠的HEAT重复序列中）对于与RanGTP或与NPC交互至关重要。此外，发现impbeta449与另一种核迁移蛋白，即β-catenin，具有结构相似性，后者由另一种类型的ARM重复的螺旋重复结构组成。有趣的是，importin-beta和beta-catenin的NPC易位的基本区域在空间上相互重叠。这有力地表明了HEAT或ARM重复序列的螺旋堆积对于NPC通道的重要性。版权所有2000学术出版社。

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