1rw2: Difference between revisions

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New page: left|200px<br /> <applet load="1rw2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rw2" /> '''Three-dimensional structure of Ku80 CTD'''<...
 
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[[Image:1rw2.gif|left|200px]]<br />
[[Image:1rw2.gif|left|200px]]<br /><applet load="1rw2" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1rw2" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1rw2" />
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'''Three-dimensional structure of Ku80 CTD'''<br />
'''Three-dimensional structure of Ku80 CTD'''<br />


==Overview==
==Overview==
The solution structure of Ku80 CTD from residue 566 to 732 has been solved, in order to gain insights into the mechanisms of its interactions with, other proteins. The structure reveals a topology similar to several common, scaffolds for protein-protein interactions, in the absence of significant, sequence similarity to these proteins. Conserved surface amino acid, residues are clustered on two main surface areas, which are likely, involved in mediating interactions between Ku80 and other proteins. The, Ku70/Ku80 heterodimer has been shown to be involved in at least three, processes, nonhomologous end joining, transcription, and telomere, maintenance, and thus it needs to interact with different proteins, involved in these different processes. The three-dimensional structure of, the Ku80 C-terminal domain and the availability of NMR chemical shift, assignments provide a basis for further investigation of the interactions, between Ku80 and other proteins in these Ku-dependent cellular functions.
The solution structure of Ku80 CTD from residue 566 to 732 has been solved in order to gain insights into the mechanisms of its interactions with other proteins. The structure reveals a topology similar to several common scaffolds for protein-protein interactions, in the absence of significant sequence similarity to these proteins. Conserved surface amino acid residues are clustered on two main surface areas, which are likely involved in mediating interactions between Ku80 and other proteins. The Ku70/Ku80 heterodimer has been shown to be involved in at least three processes, nonhomologous end joining, transcription, and telomere maintenance, and thus it needs to interact with different proteins involved in these different processes. The three-dimensional structure of the Ku80 C-terminal domain and the availability of NMR chemical shift assignments provide a basis for further investigation of the interactions between Ku80 and other proteins in these Ku-dependent cellular functions.


==About this Structure==
==About this Structure==
1RW2 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=1RW2 OCA].  
1RW2 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=1RW2 OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Cano, L.]]
[[Category: Cano, L.]]
[[Category: Chen, D.J.]]
[[Category: Chen, D J.]]
[[Category: Chen, Y.]]
[[Category: Chen, Y.]]
[[Category: Hu, W.]]
[[Category: Hu, W.]]
[[Category: Lee, T.D.]]
[[Category: Lee, T D.]]
[[Category: Zhang, Z.]]
[[Category: Zhang, Z.]]
[[Category: dna-pk]]
[[Category: dna-pk]]
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[[Category: structure]]
[[Category: structure]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:55:12 2008''

Revision as of 15:55, 21 February 2008

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1rw2

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Three-dimensional structure of Ku80 CTD

OverviewOverview

The solution structure of Ku80 CTD from residue 566 to 732 has been solved in order to gain insights into the mechanisms of its interactions with other proteins. The structure reveals a topology similar to several common scaffolds for protein-protein interactions, in the absence of significant sequence similarity to these proteins. Conserved surface amino acid residues are clustered on two main surface areas, which are likely involved in mediating interactions between Ku80 and other proteins. The Ku70/Ku80 heterodimer has been shown to be involved in at least three processes, nonhomologous end joining, transcription, and telomere maintenance, and thus it needs to interact with different proteins involved in these different processes. The three-dimensional structure of the Ku80 C-terminal domain and the availability of NMR chemical shift assignments provide a basis for further investigation of the interactions between Ku80 and other proteins in these Ku-dependent cellular functions.

About this StructureAbout this Structure

1RW2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Solution structure of the C-terminal domain of Ku80 suggests important sites for protein-protein interactions., Zhang Z, Hu W, Cano L, Lee TD, Chen DJ, Chen Y, Structure. 2004 Mar;12(3):495-502. PMID:15016365

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