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DNA repair gets physical: mapping an XPA-binding site on ERCC1.

ABSTRACT: 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.

SUBMITTER: Croteau DL

PROVIDER: S-EPMC2494945 | biostudies-literature | 2008 May

REPOSITORIES: biostudies-literature

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DNA repair gets physical: mapping an XPA-binding site on ERCC1.

Croteau Deborah L DL Peng Ye Y Van Houten Bennett B

DNA repair 20080314 5

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 impo ...[more]

PMID: 18343204

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