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1rrp

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Revision as of 11:55, 20 March 2008 by OCA (Talk | contribs)
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PDB ID 1rrp

Drag the structure with the mouse to rotate
, resolution 2.96Å
Ligands: and
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF THE RAN-GPPNHP-RANBD1 COMPLEX


Contents

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.

Disease

Known diseases associated with this structure: Osteolysis, familial expansile OMIM:[603499], Paget disease of bone OMIM:[603499]

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

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