1f4r
From Proteopedia
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CRYSTAL STRUCTURE OF THE HUMAN AAG DNA REPAIR GLYCOSYLASE COMPLEXED WITH 1,N6-ETHENOADENINE-DNA
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Overview
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-A 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.
Disease
Known disease associated with this structure: Opitz G syndrome, type I OMIM:[300552]
About this Structure
1F4R is a Single protein structure of sequence from Homo sapiens with as ligand. Active as DNA-3-methyladenine glycosylase I, with EC number 3.2.2.20 Full crystallographic information is available from OCA.
Reference
Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG., Lau AY, Wyatt MD, Glassner BJ, Samson LD, Ellenberger T, Proc Natl Acad Sci U S A. 2000 Dec 5;97(25):13573-8. PMID:11106395
Page seeded by OCA on Thu Feb 21 12:34:49 2008
