1z00: Difference between revisions

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New page: left|200px<br /> <applet load="1z00" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z00" /> '''Solution structure of the C-terminal domain...
 
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[[Image:1z00.gif|left|200px]]<br />
[[Image:1z00.gif|left|200px]]<br /><applet load="1z00" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1z00" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1z00" />
caption="1z00" />
'''Solution structure of the C-terminal domain of ERCC1 complexed with the C-terminal domain of XPF'''<br />
'''Solution structure of the C-terminal domain of ERCC1 complexed with the C-terminal domain of XPF'''<br />


==Overview==
==Overview==
The human ERCC1/XPF complex is a structure-specific endonuclease with, defined polarity that participates in multiple DNA repair pathways. We, report the heterodimeric structure of the C-terminal domains of both, proteins responsible for ERCC1/XPF complex formation. Both domains exhibit, the double helix-hairpin-helix motif (HhH)2, and they are related by a, pseudo-2-fold symmetry axis. In the XPF domain, the hairpin of the second, motif is replaced by a short turn. The ERCC1 domain folds properly only in, the presence of the XPF domain, which implies a role for XPF as a scaffold, for the folding of ERCC1. The intersubunit interactions are largely, hydrophobic in nature. NMR titration data show that only the ERCC1 domain, of the ERCC1/XPF complex is involved in DNA binding. On the basis of these, findings, we propose a model for the targeting of XPF nuclease via, ERCC1-mediated interactions in the context of nucleotide excision repair.
The human ERCC1/XPF complex is a structure-specific endonuclease with defined polarity that participates in multiple DNA repair pathways. We report the heterodimeric structure of the C-terminal domains of both proteins responsible for ERCC1/XPF complex formation. Both domains exhibit the double helix-hairpin-helix motif (HhH)2, and they are related by a pseudo-2-fold symmetry axis. In the XPF domain, the hairpin of the second motif is replaced by a short turn. The ERCC1 domain folds properly only in the presence of the XPF domain, which implies a role for XPF as a scaffold for the folding of ERCC1. The intersubunit interactions are largely hydrophobic in nature. NMR titration data show that only the ERCC1 domain of the ERCC1/XPF complex is involved in DNA binding. On the basis of these findings, we propose a model for the targeting of XPF nuclease via ERCC1-mediated interactions in the context of nucleotide excision repair.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
1Z00 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1Z00 OCA].  
1Z00 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1Z00 OCA].  


==Reference==
==Reference==
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[[Category: Das, D.]]
[[Category: Das, D.]]
[[Category: Folkers, G.]]
[[Category: Folkers, G.]]
[[Category: Hoeijmakers, J.H.J.]]
[[Category: Hoeijmakers, J H.J.]]
[[Category: Jaspers, N.G.J.]]
[[Category: Jaspers, N G.J.]]
[[Category: Kaptein, R.]]
[[Category: Kaptein, R.]]
[[Category: Odijk, H.]]
[[Category: Odijk, H.]]
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[[Category: helix-hairpin-helix]]
[[Category: helix-hairpin-helix]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:27:44 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:10:49 2008''