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  NES consensus redefined by structures of PKI-type and Rev-type nuclear export signals bound to CRM1.

Güttler, T., Madl, T., Neumann, P., Deichsel, D., Lorenzo, C., Monecke, T., et al. (2010). NES consensus redefined by structures of PKI-type and Rev-type nuclear export signals bound to CRM1. Nature Structural and Molecular Biology, 17(11), 1367-1376. Retrieved from http://www.nature.com/nsmb/journal/v17/n11/pdf/nsmb.1931.pdf.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-D4DB-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-1DC2-2
Genre: Journal Article

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Güttler, T.1, Author              
Madl, T., Author
Neumann, P., Author
Deichsel, D., Author
Lorenzo, C., Author
Monecke, T., Author
Ficner, R., Author
Sattler, M., Author
Görlich, D.1, Author              
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1Department of Cellular Logistics, MPI for biophysical chemistry, Max Planck Society, ou_578574              

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 Abstract: Classic nuclear export signals (NESs) confer CRM1-dependent nuclear export. Here we present crystal structures of the RanGTP−CRM1 complex alone and bound to the prototypic PKI or HIV-1 Rev NESs. These NESs differ markedly in the spacing of their key hydrophobic (Φ) residues, yet CRM1 recognizes them with the same rigid set of five Φ pockets. The different Φ spacings are compensated for by different conformations of the bound NESs: in the case of PKI, an α-helical conformation, and in the case of Rev, an extended conformation with a critical proline docking into a Φ pocket. NMR analyses of CRM1-bound and CRM1-free PKI NES suggest that CRM1 selects NES conformers that pre-exist in solution. Our data lead to a new structure-based NES consensus, and explain why NESs differ in their affinities for CRM1 and why supraphysiological NESs bind the exportin so tightly.

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Language(s): eng - English
 Dates: 2010-11
 Publication Status: Published in print
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Title: Nature Structural and Molecular Biology
Source Genre: Journal
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Pages: - Volume / Issue: 17 (11) Sequence Number: - Start / End Page: 1367 - 1376 Identifier: -