1ibr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
|PDB= 1ibr |SIZE=350|CAPTION= <scene name='initialview01'>1ibr</scene>, resolution 2.30&Aring;
|PDB= 1ibr |SIZE=350|CAPTION= <scene name='initialview01'>1ibr</scene>, resolution 2.30&Aring;
|SITE=
|SITE=
-
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER'>GNP</scene>
+
|LIGAND= <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ibr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ibr OCA], [http://www.ebi.ac.uk/pdbsum/1ibr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ibr RCSB]</span>
}}
}}
Line 14: Line 17:
==Overview==
==Overview==
Transport receptors of the Importin beta family shuttle between the nucleus and cytoplasm and mediate transport of macromolecules through nuclear pore complexes. They interact specifically with the GTP-binding protein Ran, which in turn regulates their interaction with cargo. Here, we report the three-dimensional structure of a complex between Ran bound to the nonhydrolyzable GTP analog GppNHp and a 462-residue fragment from Importin beta. The structure of Importin beta shows 10 tandem repeats resembling HEAT and Armadillo motifs. They form an irregular crescent, the concave site of which forms the interface with Ran-triphosphate. The importin-binding site of Ran does not overlap with that of the Ran-binding domain of RanBP2.
Transport receptors of the Importin beta family shuttle between the nucleus and cytoplasm and mediate transport of macromolecules through nuclear pore complexes. They interact specifically with the GTP-binding protein Ran, which in turn regulates their interaction with cargo. Here, we report the three-dimensional structure of a complex between Ran bound to the nonhydrolyzable GTP analog GppNHp and a 462-residue fragment from Importin beta. The structure of Importin beta shows 10 tandem repeats resembling HEAT and Armadillo motifs. They form an irregular crescent, the concave site of which forms the interface with Ran-triphosphate. The importin-binding site of Ran does not overlap with that of the Ran-binding domain of RanBP2.
- 
-
==Disease==
 
-
Known diseases associated with this structure: Osteolysis, familial expansile OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=603499 603499]], Paget disease of bone OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=603499 603499]]
 
==About this Structure==
==About this Structure==
Line 30: Line 30:
[[Category: Vetter, I R.]]
[[Category: Vetter, I R.]]
[[Category: Wittinghofer, A.]]
[[Category: Wittinghofer, A.]]
-
[[Category: GNP]]
+
[[Category: nuclear transport receptor]]
-
[[Category: MG]]
+
[[Category: small gtpase]]
-
[[Category: small gtpase; nuclear transport receptor]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:48:11 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:17:30 2008''

Revision as of 18:17, 30 March 2008


PDB ID 1ibr

Drag the structure with the mouse to rotate
, resolution 2.30Å
Ligands: ,
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



COMPLEX OF RAN WITH IMPORTIN BETA


Overview

Transport receptors of the Importin beta family shuttle between the nucleus and cytoplasm and mediate transport of macromolecules through nuclear pore complexes. They interact specifically with the GTP-binding protein Ran, which in turn regulates their interaction with cargo. Here, we report the three-dimensional structure of a complex between Ran bound to the nonhydrolyzable GTP analog GppNHp and a 462-residue fragment from Importin beta. The structure of Importin beta shows 10 tandem repeats resembling HEAT and Armadillo motifs. They form an irregular crescent, the concave site of which forms the interface with Ran-triphosphate. The importin-binding site of Ran does not overlap with that of the Ran-binding domain of RanBP2.

About this Structure

1IBR is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural view of the Ran-Importin beta interaction at 2.3 A resolution., Vetter IR, Arndt A, Kutay U, Gorlich D, Wittinghofer A, Cell. 1999 May 28;97(5):635-46. PMID:10367892

Page seeded by OCA on Sun Mar 30 21:17:30 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools