NDLI: Structural basis for leucine-rich nuclear export signal recognition by CRM1

Content Provider	PubMed Central
Author	Dong, Xiuhua Biswas, Anindita Süel, Katherine E. Jackson, Laurie K. Martinez, Rita Gu, Hongmei Min, Chook Yuh
Copyright Year	2009
Abstract	CRM1 (also known as XPO1 and exportin 1) mediates nuclear export of hundreds of proteins through the recognition of the leucine-rich nuclear export signal (LR-NES). Here we present the 2.9Å structure of CRM1 bound to snurportin 1 (SNUPN). Snurportin 1 binds CRM1 in a bipartite manner by means of an amino-terminal LR-NES and its nucleotide-binding domain. The LR-NES is a combined α-helical-extended structure that occupies a hydrophobic groove between two CRM1 outer helices. The LR-NES interface explains the consensus hydrophobic pattern, preference for intervening electronegative residues and inhibition by leptomycin B. The second nuclear export signal epitope is a basic surface on the snurportin 1 nucleotide-binding domain, which binds an acidic patch on CRM1 adjacent to the LR-NES site. Multipartite recognition of individually weak nuclear export signal epitopes may be common to CRM1 substrates, enhancing CRM1 binding beyond the generally low affinity LR-NES. Similar energetic construction is also used in multipartite nuclear localization signals to provide broad substrate specificity and rapid evolution in nuclear transport.
Related Links	http://dx.doi.org/10.1038/nature07975
Ending Page	1141
Page Count	6
Starting Page	1136
File Format	PDF
ISSN	00280836
e-ISSN	14764687
Journal	Nature
Issue Number	7242
Volume Number	458
Language	English
Publisher Date	2009-04-30
Access Restriction	Open
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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