National Center for
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
Conformational selection in the recognition of the snurportin importin beta binding domain by importin beta
Biochemistry (2010) 49 p.5042-5047
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.