Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport

Ingrid R. Vetter, Christine Nowak, Takeharu Nishimoto, Jürgen Kuhlmann and Alfred Wittinghofer ()
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Ingrid R. Vetter: Max-Planck-Institut fr molekulare Physiologie
Christine Nowak: Max-Planck-Institut fr molekulare Physiologie
Takeharu Nishimoto: Graduate School of Medical Science, Kyushu University
Jürgen Kuhlmann: Max-Planck-Institut fr molekulare Physiologie
Alfred Wittinghofer: Max-Planck-Institut fr molekulare Physiologie

Nature, 1999, vol. 398, issue 6722, 39-46

Abstract: Abstract The protein Ran is a small GTP-binding protein that binds to two types of effector inside the cell: Ran-binding proteins, which have a role in terminating export processes from the nucleus to the cytoplasm, and importin-β-like molecules that bind cargo proteins during nuclear transport. The Ran-binding domain is a conserved sequence motif found in several proteins that participate in these transport processes. The Ran-binding protein RanBP2 contains four of these domains and constitutes a large part of the cytoplasmic fibrils that extend from the nuclear-pore complex. The structure of Ran bound to a non-hydrolysable GTP analogue (Ran·GppNHp) in complex with the first Ran-binding domain (RanBD1) of human RanBP2 reveals not only that RanBD1 has a pleckstrin-homology domain fold, but also that the switch-I region of Ran·GppNHp resembles the canonical Ras·GppNHp structure and that the carboxy terminus of Ran is wrapped around RanBD1, contacting a basic patch on RanBD1 through its acidic end. This molecular ‘embrace’ enables RanBDs to sequester the Ran carboxy terminus, triggering the dissociation of Ran·GTP from importin-β-related transport factors and facilitating GTP hydrolysis by the GTPase-activating protein ranGAP. Such a mechanism represents a new type of switch mechanism and regulatory protein–protein interaction for a Ras-related protein.

Date: 1999
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DOI: 10.1038/17969

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