1xks: Difference between revisions

New page: left|200px<br /> <applet load="1xks" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xks, resolution 2.35Å" /> '''The crystal structu...
 
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[[Image:1xks.gif|left|200px]]<br />
[[Image:1xks.gif|left|200px]]<br /><applet load="1xks" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1xks" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1xks, resolution 2.35&Aring;" />
caption="1xks, resolution 2.35&Aring;" />
'''The crystal structure of the N-terminal domain of Nup133 reveals a beta-propeller fold common to several nucleoporins'''<br />
'''The crystal structure of the N-terminal domain of Nup133 reveals a beta-propeller fold common to several nucleoporins'''<br />


==Overview==
==Overview==
Nucleocytoplasmic transport occurs through nuclear pore complexes (NPCs), whose complex architecture is generated from a set of only approximately, 30 proteins, termed nucleoporins. Here, we explore the domain structure of, Nup133, a nucleoporin in a conserved NPC subcomplex that is crucial for, NPC biogenesis and is believed to form part of the NPC scaffold. We show, that human Nup133 contains two domains: a COOH-terminal domain responsible, for its interaction with its subcomplex through Nup107; and an, NH2-terminal domain whose crystal structure reveals a seven-bladed, beta-propeller. The surface properties and conservation of the Nup133, beta-propeller suggest it may mediate multiple interactions with other, proteins. Other beta-propellers are predicted in a third of all, nucleoporins. These and several other repeat-based motifs appear to be, major elements of nucleoporins, indicating a level of structural, repetition that may conceptually simplify the assembly and disassembly of, this huge protein complex.
Nucleocytoplasmic transport occurs through nuclear pore complexes (NPCs) whose complex architecture is generated from a set of only approximately 30 proteins, termed nucleoporins. Here, we explore the domain structure of Nup133, a nucleoporin in a conserved NPC subcomplex that is crucial for NPC biogenesis and is believed to form part of the NPC scaffold. We show that human Nup133 contains two domains: a COOH-terminal domain responsible for its interaction with its subcomplex through Nup107; and an NH2-terminal domain whose crystal structure reveals a seven-bladed beta-propeller. The surface properties and conservation of the Nup133 beta-propeller suggest it may mediate multiple interactions with other proteins. Other beta-propellers are predicted in a third of all nucleoporins. These and several other repeat-based motifs appear to be major elements of nucleoporins, indicating a level of structural repetition that may conceptually simplify the assembly and disassembly of this huge protein complex.


==About this Structure==
==About this Structure==
1XKS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XKS OCA].  
1XKS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XKS OCA].  


==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Berke, I.C.]]
[[Category: Berke, I C.]]
[[Category: Blobel, G.]]
[[Category: Blobel, G.]]
[[Category: Boehmer, T.]]
[[Category: Boehmer, T.]]
[[Category: Schwartz, T.U.]]
[[Category: Schwartz, T U.]]
[[Category: beta-propeller]]
[[Category: beta-propeller]]
[[Category: helical insertions]]
[[Category: helical insertions]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:55:50 2008''

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