The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
Structural basis for leucine-rich nuclear export signal recognition by CRM1
Open accessAbstract
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 2.9 Å 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.
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CRM1 Is an Export Receptor for Leucine-Rich Nuclear Export Signals
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Components and regulation of nuclear transport processes
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Metadata
- Authors
- Dong, X., Biswas, A., Süel, K. E., Jackson, L. K., Martinez, R., Gu, H., & Chook, Y. M.
- Venue
- Nature
- Published
- 2009-04-01
- Volume
- 458
- Issue
- 7242
- Pages
- 1136-1141
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1971961101
- Cited by
- 330
- References
- 48
- FWCI
- 9.60
- Type
- journal article
- Language
- en
- Open access
- green
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- Dong, X., Biswas, A., Süel, K. E., Jackson, L. K., Martinez, R., Gu, H., & Chook, Y. M. (2009). Structural basis for leucine-rich nuclear export signal recognition by CRM1. Nature. https://doi.org/10.1038/nature07975
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