Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 16, Issue 5, Pages 558-560Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1586
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Funding
- US National Institutes of Health [R01GM069909, R01GM069909-03S1, 5-T32-GM008297]
- Welch Foundation [I-1532]
- University of Texas Southwestern Endowed Scholars Program
- US Department of Energy, Office of Energy Research [W-31-109-ENG-38]
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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).
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