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Updated: Jul 16, 2026

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis
Published on: October 15, 2019
Structural and biochemical characterization of the Importin-beta.Ran.GTP.RanBD1 complex
Marc Sarić1, Xiaodong Zhao, Carolin Körner
1Max-Planck-Institute for Molecular Physiology, Department Structural Biology, Otto-Hahn-Str. 11, D-44227 Dortmund, Germany.
Abstract:
Here we present the crystal structure of Importin-beta(1-462).Ran.GTP.RanBD1DeltaN as solved by molecular replacement. HPLC dissociation measurements on this complex show, that the N-terminus of RanBD may be involved in the release of the hydrolysis- and dissociation-block of Ran by Transportin/Importin-beta. We could identify a pair of amino acids which - upon mutation - weaken the interaction between Ran and Importin-beta specifically to allow dissociation without RanBD. These findings support the hypothesis that a ternary complex of Importin-beta.Ran.GTP.RanBD exists in the final step of the export of Importin-beta from the nucleus and that interaction of the N-terminus of RanBD with Ran plays a crucial role in disassembly of this complex.
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