3NBY: Crystal Structure Of The Pki Nes-Crm1-Rangtp Nuclear Export Complex

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 (Phi) residues, yet CRM1 recognizes them with the same rigid set of five Phi pockets. The different Phi spacings are compensated for by different conformations of the bound NESs: in the case of PKI, an alpha-helical conformation, and in the case of Rev, an extended conformation with a critical proline docking into a Phi 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.
PDB ID: 3NBYDownload
MMDB ID: 85787
PDB Deposition Date: 2010/6/4
Updated in MMDB: 2010/12
Experimental Method:
x-ray diffraction
Resolution: 3.42  Å
Source Organism:
Mus musculus
Similar Structures:
Biological Unit for 3NBY: trimeric; determined by author and by software (PISA)
Molecular Components in 3NBY
Label Count Molecule
Proteins (3 molecules)
Snurportin-1(Gene symbol: SNUPN)
Molecule annotation
Gtp-binding Nuclear Protein RAN(Gene symbol: RAN)
Molecule annotation
Exportin-1(Gene symbol: Xpo1)
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB