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| {{STRUCTURE_2fc0| PDB=2fc0 | SCENE= }} | | {{STRUCTURE_2fc0| PDB=2fc0 | SCENE= }} |
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| '''WRN exonuclease, Mn dGMP complex'''
| | ===WRN exonuclease, Mn dGMP complex=== |
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| ==Overview==
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| WRN is unique among the five human RecQ DNA helicases in having a functional exonuclease domain (WRN-exo) and being defective in the premature aging and cancer-related disorder Werner syndrome. Here, we characterize WRN-exo crystal structures, biochemical activity and participation in DNA end joining. Metal-ion complex structures, active site mutations and activity assays reveal a nuclease mechanism mediated by two metal ions. The DNA end-binding Ku70/80 complex specifically stimulates WRN-exo activity, and structure-based mutational inactivation of WRN-exo alters DNA end joining in human cells. We furthermore establish structural and biochemical similarities of WRN-exo to DnaQ-family replicative proofreading exonucleases, describing WRN-specific adaptations consistent with double-stranded DNA specificity and functionally important conformational changes. These results indicate WRN-exo is a human DnaQ family member and support DnaQ-like proofreading activities stimulated by Ku70/80, with implications for WRN functions in age-related pathologies and maintenance of genomic integrity.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16622405}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16622405 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16622405}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Werner syndrome]] | | [[Category: Werner syndrome]] |
| [[Category: Wrn]] | | [[Category: Wrn]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:42:49 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:38:19 2008'' |
