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Journal Article

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

MPS-Authors
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Güttler,  T.
Department of Cellular Logistics, MPI for biophysical chemistry, Max Planck Society;

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Görlich,  D.
Department of Cellular Logistics, MPI for biophysical chemistry, Max Planck Society;

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Fulltext (public)

587581.pdf
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Supplementary Material (public)

587581_Suppl.pdf
(Supplementary material), 6MB

Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0012-D4DB-B
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.