1rrp

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spinqualitylabelsall models 1rrp, resolution 2.96Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURE OF THE RAN-GPPNHP-RANBD1 COMPLEX

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

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 with MG and GNP as ligands. 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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