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| [[Image:1fu1.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1fu1| PDB=1fu1 | SCENE= }} | | {{STRUCTURE_1fu1| PDB=1fu1 | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF HUMAN XRCC4'''
| | ===CRYSTAL STRUCTURE OF HUMAN XRCC4=== |
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| ==Overview==
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| XRCC4 is essential for carrying out non-homologous DNA end joining (NHEJ) in all eukaryotes and, in particular, V(D)J recombination in vertebrates. Xrcc4 protein forms a complex with DNA ligase IV that rejoins two DNA ends in the last step of V(D)J recombination and NHEJ to repair double strand breaks. XRCC4-defective cells are extremely sensitive to ionizing radiation, and disruption of the XRCC4 gene results in embryonic lethality in mice. Here we report the crystal structure of a functional fragment of Xrcc4 at 2.7 A resolution. Xrcc4 protein forms a strikingly elongated dumb-bell-like tetramer. Each of the N-terminal globular head domains consists of a beta-sandwich and a potentially DNA-binding helix- turn-helix motif. The C-terminal stalk comprising a single alpha-helix >120 A in length is partly incorporated into a four-helix bundle in the Xrcc4 tetramer and partly involved in interacting with ligase IV. The Xrcc4 structure suggests a possible mode of coupling ligase IV association with DNA binding for effective ligation of DNA ends.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11080143}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11080143 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11080143}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Helix bundle]] | | [[Category: Helix bundle]] |
| [[Category: Helix-turn-helix]] | | [[Category: Helix-turn-helix]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:45:54 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:56:56 2008'' |
