1rrp: Difference between revisions

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[[Image:1rrp.jpg|left|200px]]
{{Seed}}
[[Image:1rrp.png|left|200px]]


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{{STRUCTURE_1rrp|  PDB=1rrp  |  SCENE=  }}  
{{STRUCTURE_1rrp|  PDB=1rrp  |  SCENE=  }}  


'''STRUCTURE OF THE RAN-GPPNHP-RANBD1 COMPLEX'''
===STRUCTURE OF THE RAN-GPPNHP-RANBD1 COMPLEX===




==Overview==
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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.
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{{ABSTRACT_PUBMED_10078529}}


==About this Structure==
==About this Structure==
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[[Category: Nuclear transport]]
[[Category: Nuclear transport]]
[[Category: Small gtpase]]
[[Category: Small gtpase]]
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