CRM1核输出复合物组装和解聚的结构基础。
Structural basis for assembly and disassembly of the CRM1 nuclear export complex.
作者信息
Dong Xiuhua, Biswas Anindita, Chook Yuh Min
机构信息
Department of Pharmacology, University of Texas Southwestern Medical Center at Dallas, USA.
出版信息
Nat Struct Mol Biol. 2009 May;16(5):558-60. doi: 10.1038/nsmb.1586. Epub 2009 Apr 1.
Abstract
CRM1 (or exportin 1, Xpo1) transports proteins out of the cell nucleus through the nuclear pore complex. In the cytoplasm, GTP hydrolysis and consequent dissociation of Ran from CRM1 releases low-affinity substrates, while additional factors facilitate release of high-affinity substrates. Here we provide a model for human CRM1 export complex assembly and disassembly through structural and biochemical analyses of CRM1 bound to the substrate snurportin 1 (SNUPN, also called snuportin 1).
摘要
CRM1（或输出蛋白1，Xpo1）通过核孔复合体将蛋白质转运出细胞核。在细胞质中，GTP水解以及随后Ran与CRM1的解离会释放低亲和力底物，而其他因子则促进高亲和力底物的释放。在这里，我们通过对与底物snurportin 1（SNUPN，也称为snuportin 1）结合的CRM1进行结构和生化分析，提供了一个人类CRM1输出复合体组装和解聚的模型。
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