3LWW: Structure Of An Open And Closed Conformation Of Human Importin Beta Bound To The Snurportin1 Ibb-Domain Trapped In The Same Crystallographic Asymmetric Unit

The structural flexibility of beta-karyopherins is critical to mediate the interaction with transport substrates, nucleoporins, and the GTPase Ran. In this paper, we provide structural evidence that the molecular recognition of the transport adaptor snurportin by importin beta follows the population selection mechanism. We have captured two drastically different conformations of importin beta bound to the snurportin importin beta binding domain trapped in the same crystallographic asymmetric unit. We propose the population selection may be a general mechanism used by beta-karyopherins to recognize transport substrates.
PDB ID: 3LWWDownload
MMDB ID: 82487
PDB Deposition Date: 2010/2/24
Updated in MMDB: 2010/06
Experimental Method:
x-ray diffraction
Resolution: 3.15  Å
Source Organism:
Similar Structures:
Biological Unit for 3LWW: dimeric; determined by author and by software (PISA)
Molecular Components in 3LWW
Label Count Molecule
Proteins (2 molecules)
Importin Subunit Beta-1(Gene symbol: KPNB1)
Molecule annotation
Snurportin-1(Gene symbol: SNUPN)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB