1l2n: Difference between revisions

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[[Image:1l2n.jpg|left|200px]]<br /><applet load="1l2n" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1l2n.jpg|left|200px]]<br /><applet load="1l2n" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1l2n" />

'''Smt3 Solution Structure'''<br />

==Overview==

Smt3 belongs to a growing family of ubiquitin-related proteins involved in, posttranslational protein modification. Independent studies demonstrate an, essential function of Smt3 in the regulation of nucleocytoplasmic, transport, and suggest a role in cell-cycle regulation. Here we report the, high-resolution NMR structure of yeast Smt3 in the complex free form. Our, comparison of the Smt3 NMR structure with the Smt3 crystal structure in, complex with the C-Terminal Ulp1 protease domain revealed large structural, differences in the binding surface, which is also involved in the, Smt3-Ubc-9 interaction detected by NMR. The structural differences in the, region indicate the important functions of conserved residues in less, structurally defined sequences.

Smt3 belongs to a growing family of ubiquitin-related proteins involved in posttranslational protein modification. Independent studies demonstrate an essential function of Smt3 in the regulation of nucleocytoplasmic transport, and suggest a role in cell-cycle regulation. Here we report the high-resolution NMR structure of yeast Smt3 in the complex free form. Our comparison of the Smt3 NMR structure with the Smt3 crystal structure in complex with the C-Terminal Ulp1 protease domain revealed large structural differences in the binding surface, which is also involved in the Smt3-Ubc-9 interaction detected by NMR. The structural differences in the region indicate the important functions of conserved residues in less structurally defined sequences.

==About this Structure==

1L2N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1L2N OCA].

1L2N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L2N OCA].

==Reference==

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[[Category: ubiquitin-like protein]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 20~~:11:~~40 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:40:38 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1l2n.jpg|left|200px]]<br /><applet load="1l2n" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1l2n.jpg|left|200px]]<br /><applet load="1l2n" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1l2n" />
 '''Smt3 Solution Structure'''<br />
 ==Overview==
-Smt3 belongs to a growing family of ubiquitin-related proteins involved in, posttranslational protein modification. Independent studies demonstrate an, essential function of Smt3 in the regulation of nucleocytoplasmic, transport, and suggest a role in cell-cycle regulation. Here we report the, high-resolution NMR structure of yeast Smt3 in the complex free form. Our, comparison of the Smt3 NMR structure with the Smt3 crystal structure in, complex with the C-Terminal Ulp1 protease domain revealed large structural, differences in the binding surface, which is also involved in the, Smt3-Ubc-9 interaction detected by NMR. The structural differences in the, region indicate the important functions of conserved residues in less, structurally defined sequences.
+Smt3 belongs to a growing family of ubiquitin-related proteins involved in posttranslational protein modification. Independent studies demonstrate an essential function of Smt3 in the regulation of nucleocytoplasmic transport, and suggest a role in cell-cycle regulation. Here we report the high-resolution NMR structure of yeast Smt3 in the complex free form. Our comparison of the Smt3 NMR structure with the Smt3 crystal structure in complex with the C-Terminal Ulp1 protease domain revealed large structural differences in the binding surface, which is also involved in the Smt3-Ubc-9 interaction detected by NMR. The structural differences in the region indicate the important functions of conserved residues in less structurally defined sequences.
 ==About this Structure==
-L2N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L2N OCA].
+L2N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L2N OCA].
 ==Reference==
@@ Line 20: / Line 20: @@
 [[Category: ubiquitin-like protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:11:40 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:40:38 2008''