@inbook{d2c4188eca83482a8ebd2c86d34a28f3,
title = "Crystallizing thoughts about DNA base excision repair",
abstract = "Chemically damaged bases are removed from DNA by glycosylases that locate the damage and cleave the bond between the modified base and the deoxyribose sugar of the DNA backbone. The detection of damaged bases in DNA poses two problems: (1) The aberrant bases are mostly buried within the double helix, and (2) a wide variety of chemically different modifications must be efficiently recognized and removed. The human alkyladenine glycosylase (AAG) and Escherichia coli AlkA DNA glycosylases excise many different types of alkylated bases from DNA. Crystal structures of these enzymes show how substrate bases are exposed to the enzyme active site and they suggest mechanisms of catalytic specificity. Both enzymes bend DNA and flip substrate bases out of the double helix and into the enzyme active site for cleavage. Although AAG and AlkA have very different overall folds, some common features of their substrate-binding sites suggest related strategies for the selective recognition of a chemically diverse group of alkylated substrates.",
author = "Thomas Hollis and Albert Lau and Tom Ellenberger",
note = "Funding Information: We thank our many colleagues and collaborators who have taught us about the intricacies of DNA damage and repair. A special thanks to Yoshi Ichikawa, Leona Samson, Orlando Sch~irer, and Greg Verdine for championing our efforts to grow crystals. Our work on DNA repair enzymes has been supported by grants from the National Institutes of Health, the Lucille P. Markey Foundation, and the Armenise-Harvard Foundation for Advanced Biomedical Research.",
year = "2001",
doi = "10.1016/s0079-6603(01)68109-1",
language = "English (US)",
isbn = "0125400683",
series = "Progress in Nucleic Acid Research and Molecular Biology",
publisher = "Academic Press Inc.",
pages = "305--314",
booktitle = "Base Excesion Repair",
}