1f59: Difference between revisions

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[[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="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1f59, resolution 2.8Å" />

'''IMPORTIN-BETA-FXFG NUCLEOPORIN COMPLEX'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1F59 OCA].

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==

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[[Category: protein-protein complex]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov~~ 12 16:49:~~17 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:35:01 2008''

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@@ 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="450" color="white" frame="true" align="right" spinBox="true"
 caption="1f59, resolution 2.8&Aring;" />
 '''IMPORTIN-BETA-FXFG NUCLEOPORIN COMPLEX'''<br />
 ==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.
+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==
-F59 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F59 OCA].
+F59 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==
@@ Line 20: / Line 19: @@
 [[Category: protein-protein complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:49:17 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:35:01 2008''