3NBY

Crystal structure of the PKI NES-CRM1-RanGTP nuclear export complex

Summary for 3NBY

• Entry DOI: 10.2210/pdb3nby/pdb
• Descriptor: Snurportin-1, GTP-binding nuclear protein Ran, Exportin-1, ... (5 entities in total)
• Functional Keywords: protein transport, gtp-binding protein-transport protein complex, gtp-binding protein/transport protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm (By similarity): O95149; Nucleus: P62826 Q6P5F9
• Total number of polymer chains: 6
• Total formula weight: 370671.65

Authors

Guttler, T.,Madl, T.,Neumann, P.,Deichsel, D.,Corsini, L.,Monecke, T.,Ficner, R.,Sattler, M.,Gorlich, D. (deposition date: 2010-06-04, release date: 2010-10-27, Last modification date: 2023-09-06)

Primary citation

Guttler, T.,Madl, T.,Neumann, P.,Deichsel, D.,Corsini, L.,Monecke, T.,Ficner, R.,Sattler, M.,Gorlich, D.
NES consensus redefined by structures of PKI-type and Rev-type nuclear export signals bound to CRM1.
Nat.Struct.Mol.Biol., 17:1367-1376, 2010

PubMed 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.

PubMed: 20972448
DOI: 10.1038/nsmb.1931

Experimental method

X-RAY DIFFRACTION (3.42 Å)