1f59
From Proteopedia
(New page: 200px<br /> <applet load="1f59" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f59, resolution 2.8Å" /> '''IMPORTIN-BETA-FXFG N...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1f59.gif|left|200px]]<br /> | + | [[Image:1f59.gif|left|200px]]<br /><applet load="1f59" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1f59" size=" | + | |
caption="1f59, resolution 2.8Å" /> | caption="1f59, resolution 2.8Å" /> | ||
'''IMPORTIN-BETA-FXFG NUCLEOPORIN COMPLEX'''<br /> | '''IMPORTIN-BETA-FXFG NUCLEOPORIN COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We describe the crystal structure of a complex between importin-beta | + | 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== | ==About this Structure== | ||
| - | 1F59 is a [http://en.wikipedia.org/wiki/Single_protein 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:// | + | 1F59 is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
| Line 20: | Line 19: | ||
[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:35:01 2008'' |
Revision as of 10:35, 21 February 2008
|
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
Page seeded by OCA on Thu Feb 21 12:35:01 2008
