Biochemistry. 2010 Jun 22;49(24):5042-7. doi: 10.1021/bi100292y.

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

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Department of Biochemistry and Molecular Biology, Thomas Jefferson University, 233 South 10th Street, Philadelphia, Pennsylvania 19107, USA.

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.

PMID:: 20476751; [PubMed - indexed for MEDLINE]

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Research Support, N.I.H., Extramural

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Grant Support

GM074846-01A1/GM/NIGMS NIH HHS/United States

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Cited by 2 PubMed Central articles

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Structures reported by this article

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

PDB: 3LWW

Source: Homo sapiens

Method: X-Ray Diffraction

Resolution: 3.15 Å

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