Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 97, Issue 25, Pages 13573-13578Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.97.25.13573
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Funding
- NCI NIH HHS [F32 CA073135] Funding Source: Medline
- NIEHS NIH HHS [K22 ES000333-01] Funding Source: Medline
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The human 3-methyladenine DNA glycosylase [alkyladenine DNA glycosylase (AAG)] catalyzes the first step of base excision repair by cleaving damaged bases from DNA. Unlike other DNA glycosylases that are specific for a particular type of damaged base, AAG excises a chemically diverse selection of substrate bases damaged by alkylation or deamination. The 2.1-Angstrom, crystal structure of AAG complexed to DNA containing 1,N-6-ethenoadenine suggests how modified bases can be distinguished from normal DNA bases in the enzyme active site. Mutational analyses of residues contacting the alkylated base in the crystal structures suggest that the shape of the damaged base, its hydrogen-bonding characteristics, and its aromaticity all contribute to the selective recognition of damage by AAG.
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