Department of Biochemistry and Molecular Biology, Thomas Jefferson University, 233 South 10th Street, Philadelphia, Pennsylvania 19107, USA.
Biochemistry. 2010 Jun 22;49(24):5042-7. doi: 10.1021/bi100292y.
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.
β-核孔蛋白的结构灵活性对于介导与转运底物、核孔蛋白和 GTP 酶 Ran 的相互作用至关重要。在本文中，我们提供了结构证据，表明转运适配器 snurportin 与 importinβ 的分子识别遵循群体选择机制。我们已经捕获了结合在同一个晶体学不对称单元中的 snurportin importinβ 结合域的 importinβ 结合的两种截然不同的构象。我们提出，群体选择可能是β-核孔蛋白识别转运底物的一种通用机制。
