ArticleBiochemistry2010
Conformational selection in the recognition of the snurportin importin beta binding domain by importin beta.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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Who cites it
14 citing papers in PubMed.
- Ran modulates allosteric crosstalk between importin β surfaces.Nature communications · 2025Article
- Sphingosine simultaneously inhibits nuclear import and activates PP2A by binding importins and PPP2R1A.The EMBO journal · 2025Article
- Ibetazol, a novel inhibitor of importin β1-mediated nuclear import.Communications biology · 2024Article
- Binding stoichiometry and structural model of the HIV-1 Rev/importin β complex.Life science alliance · 2022Article
- Article
- Review
- Enriching Traditional Protein-protein Interaction Networks with Alternative Conformations of Proteins.Scientific reports · 2017Article
- Importin β Can Bind Hepatitis B Virus Core Protein and Empty Core-Like Particles and Induce Structural Changes.PLoS pathogens · 2016Article
- MD simulations and FRET reveal an environment-sensitive conformational plasticity of importin-β.Biophysical journal · 2015Article
- Identification and characterization of Drosophila Snurportin reveals a role for the import receptor Moleskin/importin-7 in snRNP biogenesis.Molecular biology of the cell · 2013Article
- Structural basis for the nuclear export activity of Importin13.The EMBO journal · 2013Article
- Interaction of the HIV-1 intasome with transportin 3 protein (TNPO3 or TRN-SR2).The Journal of biological chemistry · 2012Article
- The importin β binding domain as a master regulator of nucleocytoplasmic transport.Biochimica et biophysica acta · 2011Review
- Structure of Importin13-Ubc9 complex: nuclear import and release of a key regulator of sumoylation.The EMBO journal · 2011Article
Corrections and comments
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Authors and funding
2 authors.
Funding
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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Registered trials
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