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Structural and biochemical characterization of the Importin-beta.Ran.GTP.RanBD1 complex |
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| Authors: | Sarić Marc Zhao Xiaodong Körner Carolin Nowak Christine Kuhlmann Jürgen Vetter Ingrid R |
| Institution: | Max-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. |
| Keywords: | f l full-length wt wild-type RanBP Ran binding protein RanBD Ran binding domain Imp-β Importin-β Imp-α Importin-α RanGAP Ran GTPase activating protein HPLC high performance liquid chromatography GTP guanosine-tri-phosphate mGTP mant-GTP GDP guanosine-di-phosphate NPC nuclear pore complex RT room temperature IBB Importin-β-binding domain of Importin-α GST glutathione-S-transferase |
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