期刊
DNA REPAIR
卷 7, 期 5, 页码 819-826出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.dnarep.2008.01.018
关键词
DNA repair; nucleotide excision repair; ERCC1; XPA; NMR; X-ray crystallography; structure-function
资金
- Intramural NIH HHS [Z01 ES061060-09] Funding Source: Medline
Two recent reports provide new physical information on how the XPA protein recruits the ERCC1-XPF heterodimer to the site of damage during the process of mammalian nucleotide excision repair (NER). Using chemical shift perturbation NMR experiments, the contact sites between a central fragment of ERCC1 and an XPA fragment have been mapped. While both studies agree with regard to the XPA-binding site, they differ on whether the ERCC1-XPA complex can simultaneously bind DNA. These studies have important implications for both the molecular process and the design of potential inhibitors of NER. Published by Elsevier B.V.
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