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      Conformational selection in the recognition of the snurportin importin beta binding domain by importin beta.

        1 ,
      Biochemistry
      American Chemical Society (ACS)

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          Abstract

          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.

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          Author and article information

          Journal
          Biochemistry
          Biochemistry
          American Chemical Society (ACS)
          1520-4995
          0006-2960
          Jun 22 2010
          : 49
          : 24
          Affiliations
          [1 ] Department of Biochemistry and Molecular Biology, Thomas Jefferson University, 233 South 10th Street, Philadelphia, Pennsylvania 19107, USA.
          Article
          NIHMS973975
          10.1021/bi100292y
          6013741
          20476751
          1ce32be2-3cd6-4f9f-aa17-17cb7be4989f
          History

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