1RRP

STRUCTURE OF THE RAN-GPPNHP-RANBD1 COMPLEX

Summary for 1RRP

• Entry DOI: 10.2210/pdb1rrp/pdb
• Descriptor: RAN, NUCLEAR PORE COMPLEX PROTEIN NUP358, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: complex (small gtpase-nuclear protein), small gtpase, nuclear transport, complex (small gtpase-nuclear protein) complex, complex (small gtpase/nuclear protein)
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P62826; Nucleus, nuclear pore complex: P49792
• Total number of polymer chains: 4
• Total formula weight: 78866.69

Authors

Vetter, I.R.,Nowak, C.,Nishimoto, T.,Kuhlmann, J.,Wittinghofer, A. (deposition date: 1999-01-15, release date: 1999-05-18, Last modification date: 2024-04-03)

Primary citation

Vetter, I.R.,Nowak, C.,Nishimoto, T.,Kuhlmann, J.,Wittinghofer, A.
Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport.
Nature, 398:39-46, 1999

PubMed 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-beta-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 x 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 x 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 x GTP from importin-beta-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.

PubMed: 10078529
DOI: 10.1038/17969

Experimental method

X-RAY DIFFRACTION (2.96 Å)