1rrp
From Proteopedia
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| - | [[Image:1rrp.jpg|left|200px]] | + | [[Image:1rrp.jpg|left|200px]] |
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| - | '''STRUCTURE OF THE RAN-GPPNHP-RANBD1 COMPLEX''' | + | {{Structure |
| + | |PDB= 1rrp |SIZE=350|CAPTION= <scene name='initialview01'>1rrp</scene>, resolution 2.96Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER'>GNP</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF THE RAN-GPPNHP-RANBD1 COMPLEX''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1RRP is a [ | + | 1RRP is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RRP OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10078529 10078529] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: small gtpase]] | [[Category: small gtpase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:55:22 2008'' |
Revision as of 11:55, 20 March 2008
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| , resolution 2.96Å | |||||||
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| 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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