The structure of importin-β bound to SREBP-2:: Nuclear import of a transcription factor
The structure of importin-β bound to SREBP-2:: Nuclear import of a transcription factor
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DOI：
10.1126/science.1088372
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发表时间：
2003-11-28
期刊：
影响因子：
56.9
通讯作者：
Yoneda, Y
中科院分区：
文献类型：
--
作者：
Lee, SJ;Sekimoto, T;Yoneda, Y
固醇调节元件结合蛋白2（SREBP-2）是胆固醇代谢所必需的核转录因子，通过其螺旋-环-螺旋亮氨酸拉链结构域与输入蛋白-β的直接相互作用进入细胞核。我们显示了与SREBP-2的活性形式复合的importin-beta的晶体结构。Importin-beta使用像一双筷子一样的长螺旋与SREBP-2二聚体相互作用。Importin-beta改变其构象，揭示其表面结构的伪双重对称性，以便它可以容纳对称的二聚体分子。Importin-beta可能使用类似的策略来识别其他二聚体货物。
The sterol regulatory element - binding protein 2 (SREBP-2), a nuclear transcription factor that is essential for cholesterol metabolism, enters the nucleus through a direct interaction of its helix-loop-helix leucine zipper domain with importin-beta. We show the crystal structure of importin-beta complexed with the active form of SREBP-2. Importin-beta uses characteristic long helices like a pair of chopsticks to interact with an SREBP-2 dimer. Importin-beta changes its conformation to reveal a pseudo-twofold symmetry on its surface structure so that it can accommodate a symmetric dimer molecule. Importin-beta may use a similar strategy to recognize other dimeric cargoes.