1rrp
From Proteopedia
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'''STRUCTURE OF THE RAN-GPPNHP-RANBD1 COMPLEX''' | '''STRUCTURE OF THE RAN-GPPNHP-RANBD1 COMPLEX''' | ||
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[[Category: Vetter, I R.]] | [[Category: Vetter, I R.]] | ||
[[Category: Wittinghofer, A.]] | [[Category: Wittinghofer, A.]] | ||
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| - | + | [[Category: Small gtpase]] | |
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Revision as of 04:50, 3 May 2008
STRUCTURE OF THE RAN-GPPNHP-RANBD1 COMPLEX
Overview
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.
About this Structure
1RRP is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport., Vetter IR, Nowak C, Nishimoto T, Kuhlmann J, Wittinghofer A, Nature. 1999 Mar 4;398(6722):39-46. PMID:10078529 Page seeded by OCA on Sat May 3 07:50:01 2008
