The ligand binding preferences, structural features, and biological function of SH3 (Src homology 3) domains are discussed. SH3 domains bind ''core'' Pro-rich peptide ligands (7-9 amino acids in length) in a polyproline II helical conformation in a highly conserved aromatic rich patch on the protein
3-methyladenine DNA glycosylases: structure, function, and biological importance
β Scribed by Michael D. Wyatt; James M. Allan; Albert Y. Lau; Tom E. Ellenberger; Leona D. Samson
- Publisher
- John Wiley and Sons
- Year
- 1999
- Tongue
- English
- Weight
- 121 KB
- Volume
- 21
- Category
- Article
- ISSN
- 0265-9247
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β¦ Synopsis
The genome continuously suffers damage due to its reactivity with chemical and physical agents. Finding such damage in genomes (that can be several million to several billion nucleotide base pairs in size) is a seemingly daunting task. 3-Methyladenine DNA glycosylases can initiate the base excision repair (BER) of an extraordinarily wide range of substrate bases. The advantage of such broad substrate recognition is that these enzymes provide resistance to a wide variety of DNA damaging agents; however, under certain circumstances, the eclectic nature of these enzymes can confer some biological disadvantages. Solving the X-ray crystal structures of two 3-methyladenine DNA glycosylases, and creating cells and animals altered for this activity, contributes to our understanding of their enzyme mechanism and how such enzymes influence the biological response of organisms to several different types of DNA damage.
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