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Crystal structure of the metazoan Nup62•Nup58•Nup54 nucleoporin complex.

MPG-Autoren
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Chug,  H.
Department of Cellular Logistics, MPI for Biophysical Chemistry, Max Planck Society;

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Trakhanov,  S.
Department of Cellular Logistics, MPI for Biophysical Chemistry, Max Planck Society;

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Hülsmann,  B. B.
Department of Cellular Logistics, MPI for Biophysical Chemistry, Max Planck Society;

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Pleiner,  T.
Department of Cellular Logistics, MPI for Biophysical Chemistry, Max Planck Society;

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Görlich,  D.
Department of Cellular Logistics, MPI for Biophysical Chemistry, Max Planck Society;

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Zitation

Chug, H., Trakhanov, S., Hülsmann, B. B., Pleiner, T., & Görlich, D. (2015). Crystal structure of the metazoan Nup62•Nup58•Nup54 nucleoporin complex. Science, 350(6256), 106-110. doi:10.1126/science.aac7420.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0028-4F55-3
Zusammenfassung
Nuclear pore complexes (NPCs) conduct nucleocytoplasmic transport and gain transport selectivity through nucleoporin FG domains. Here, we report a structural analysis of the FG Nup62•58•54 complex, which is a crucial component of the transport system. It comprises a ≈13 nm long trimerization interface with an unusual 2W3F coil, a canonical heterotrimeric coiled coil, and a kink that enforces a compact six-helix bundle. Nup54 also contains a ferredoxin-like domain. We further identified a heterotrimeric Nup93-binding module for NPC anchorage. The quaternary structure alternations in the Nup62 complex, which were previously proposed to trigger a general NPC-gating, are incompatible with the trimer structure. We suggest that the highly elongated Nup62 complex projects barrier-forming FG-repeats far into the central NPC channel, supporting a barrier that guards the entire cross-section.