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Nat Struct Mol Biol. 2010 Nov;17(11):1367-76. doi: 10.1038/nsmb.1931. Epub 2010 Oct 24.

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

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  • 1Max-Planck-Institut für Biophysikalische Chemie, Göttingen, Germany.

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.

Comment in

  • Solving the NES problem. [Nat Struct Mol Biol. 2010]
PMID:
20972448
[PubMed - indexed for MEDLINE]
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