1f59: Difference between revisions
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[[Image:1f59.gif|left|200px]] | [[Image:1f59.gif|left|200px]] | ||
'''IMPORTIN-BETA-FXFG NUCLEOPORIN COMPLEX''' | {{Structure | ||
|PDB= 1f59 |SIZE=350|CAPTION= <scene name='initialview01'>1f59</scene>, resolution 2.8Å | |||
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|LIGAND= | |||
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'''IMPORTIN-BETA-FXFG NUCLEOPORIN COMPLEX''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1F59 is a [ | 1F59 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F59 OCA]. | ||
==Reference== | ==Reference== | ||
Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking., Bayliss R, Littlewood T, Stewart M, Cell. 2000 Jul 7;102(1):99-108. PMID:[http:// | Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking., Bayliss R, Littlewood T, Stewart M, Cell. 2000 Jul 7;102(1):99-108. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10929717 10929717] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
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[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
''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 11:04:36 2008'' | ||
Revision as of 09:04, 20 March 2008
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| 1f59, resolution 2.8Å | |||||||||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
IMPORTIN-BETA-FXFG NUCLEOPORIN COMPLEX
Overview
We describe the crystal structure of a complex between importin-beta residues 1-442 (Ib442) and five FxFG nucleoporin repeats from Nsp1p. Nucleoporin FxFG cores bind on the convex face of Ib442 to a primary site between the A helices of HEAT repeats 5 and 6, and to a secondary site between HEAT repeats 6 and 7. Mutations at importin-beta Ile178 in the primary FxFG binding site reduce both binding and nuclear protein import, providing direct evidence for the functional significance of the importin-beta-FxFG interaction. The FxFG binding sites on importin-beta do not overlap with the RanGTP binding site. Instead, RanGTP may release importin-beta from FxFG nucleoporins by generating a conformational change that alters the structure of the FxFG binding site.
About this Structure
1F59 is a Single protein structure of sequence from Homo sapiens and Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking., Bayliss R, Littlewood T, Stewart M, Cell. 2000 Jul 7;102(1):99-108. PMID:10929717
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