1f4r

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[[Image:1f4r.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_1f4r| PDB=1f4r | SCENE= }}
{{STRUCTURE_1f4r| PDB=1f4r | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE HUMAN AAG DNA REPAIR GLYCOSYLASE COMPLEXED WITH 1,N6-ETHENOADENINE-DNA'''
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===CRYSTAL STRUCTURE OF THE HUMAN AAG DNA REPAIR GLYCOSYLASE COMPLEXED WITH 1,N6-ETHENOADENINE-DNA===
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==Overview==
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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-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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11106395 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11106395}}
==About this Structure==
==About this Structure==
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[[Category: Wyatt, M D.]]
[[Category: Wyatt, M D.]]
[[Category: Protein-dna complex]]
[[Category: Protein-dna complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:41:27 2008''

Revision as of 23:41, 30 June 2008

Template:STRUCTURE 1f4r

CRYSTAL STRUCTURE OF THE HUMAN AAG DNA REPAIR GLYCOSYLASE COMPLEXED WITH 1,N6-ETHENOADENINE-DNA

Template:ABSTRACT PUBMED 11106395

About this Structure

1F4R is a Single protein structure of sequence from Homo sapiens. 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

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