2r9a
From Proteopedia
(New page: 200px<br /><applet load="2r9a" size="350" color="white" frame="true" align="right" spinBox="true" caption="2r9a, resolution 2.50Å" /> '''Crystal structure of...) |
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==Overview== | ==Overview== | ||
| - | DNA double-strand breaks represent one of the most severe forms of DNA | + | DNA double-strand breaks represent one of the most severe forms of DNA damage in mammalian cells. One pathway for repairing these breaks occurs via nonhomologous end-joining (NHEJ) and depends on XRCC4, LigaseIV, and Cernunnos, also called XLF. Although XLF stimulates XRCC4/LigaseIV to ligate mismatched and noncohesive DNA ends, the mechanistic basis for this function remains unclear. Here we report the structure of a partially functional 224 residue N-terminal fragment of human XLF. Despite only weak sequence similarity, XLF(1-170) shares structural homology with XRCC4(1-159). However, unlike the highly extended 130 A helical domain observed in XRCC4, XLF adopts a more compact, folded helical C-terminal region involving two turns and a twist, wrapping back to the structurally conserved N terminus. Mutational analysis of XLF and XRCC4 reveals a potential interaction interface, suggesting a mechanism for how XLF stimulates the ligation of mismatched ends. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Crystal | + | Crystal structure of human XLF: a twist in nonhomologous DNA end-joining., Andres SN, Modesti M, Tsai CJ, Chu G, Junop MS, Mol Cell. 2007 Dec 28;28(6):1093-101. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18158905 18158905] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Andres, S | + | [[Category: Andres, S N.]] |
| - | [[Category: Junop, M | + | [[Category: Junop, M S.]] |
[[Category: alternative splicing]] | [[Category: alternative splicing]] | ||
[[Category: cernunnos]] | [[Category: cernunnos]] | ||
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[[Category: xlf]] | [[Category: xlf]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:45:37 2008'' |
Revision as of 16:45, 21 February 2008
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Crystal structure of human XLF
Overview
DNA double-strand breaks represent one of the most severe forms of DNA damage in mammalian cells. One pathway for repairing these breaks occurs via nonhomologous end-joining (NHEJ) and depends on XRCC4, LigaseIV, and Cernunnos, also called XLF. Although XLF stimulates XRCC4/LigaseIV to ligate mismatched and noncohesive DNA ends, the mechanistic basis for this function remains unclear. Here we report the structure of a partially functional 224 residue N-terminal fragment of human XLF. Despite only weak sequence similarity, XLF(1-170) shares structural homology with XRCC4(1-159). However, unlike the highly extended 130 A helical domain observed in XRCC4, XLF adopts a more compact, folded helical C-terminal region involving two turns and a twist, wrapping back to the structurally conserved N terminus. Mutational analysis of XLF and XRCC4 reveals a potential interaction interface, suggesting a mechanism for how XLF stimulates the ligation of mismatched ends.
About this Structure
2R9A is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of human XLF: a twist in nonhomologous DNA end-joining., Andres SN, Modesti M, Tsai CJ, Chu G, Junop MS, Mol Cell. 2007 Dec 28;28(6):1093-101. PMID:18158905
Page seeded by OCA on Thu Feb 21 18:45:37 2008
