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- W2042551931 endingPage "258" @default.
- W2042551931 startingPage "249" @default.
- W2042551931 abstract "DNA N-glycosylases are base excision-repair proteins that locate and cleave damaged bases from DNA as the first step in restoring the genetic blueprint. The human enzyme 3-methyladenine DNA glycosylase removes a diverse group of damaged bases from DNA, including cytotoxic and mutagenic alkylation adducts of purines. We report the crystal structure of human 3-methyladenine DNA glycosylase complexed to a mechanism-based pyrrolidine inhibitor. The enzyme has intercalated into the minor groove of DNA, causing the abasic pyrrolidine nucleotide to flip into the enzyme active site, where a bound water is poised for nucleophilic attack. The structure shows an elegant means of exposing a nucleotide for base excision as well as a network of residues that could catalyze the in-line displacement of a damaged base from the phosphodeoxyribose backbone." @default.
- W2042551931 created "2016-06-24" @default.
- W2042551931 creator A5016887081 @default.
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- W2042551931 creator A5043175949 @default.
- W2042551931 creator A5047514569 @default.
- W2042551931 creator A5056306966 @default.
- W2042551931 date "1998-10-01" @default.
- W2042551931 modified "2023-10-16" @default.
- W2042551931 title "Crystal Structure of a Human Alkylbase-DNA Repair Enzyme Complexed to DNA" @default.
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- W2042551931 doi "https://doi.org/10.1016/s0092-8674(00)81755-9" @default.
- W2042551931 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9790531" @default.
- W2042551931 hasPublicationYear "1998" @default.
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