1f4r

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[[Image:1f4r.gif|left|200px]]<br /><applet load="1f4r" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1f4r.gif|left|200px]]
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caption="1f4r, resolution 2.4&Aring;" />
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'''CRYSTAL STRUCTURE OF THE HUMAN AAG DNA REPAIR GLYCOSYLASE COMPLEXED WITH 1,N6-ETHENOADENINE-DNA'''<br />
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{{Structure
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|PDB= 1f4r |SIZE=350|CAPTION= <scene name='initialview01'>1f4r</scene>, resolution 2.4&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NA:SODIUM ION'>NA</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/DNA-3-methyladenine_glycosylase_I DNA-3-methyladenine glycosylase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.20 3.2.2.20]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF THE HUMAN AAG DNA REPAIR GLYCOSYLASE COMPLEXED WITH 1,N6-ETHENOADENINE-DNA'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1F4R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/DNA-3-methyladenine_glycosylase_I DNA-3-methyladenine glycosylase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.20 3.2.2.20] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F4R OCA].
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1F4R is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F4R OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11106395 11106395]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11106395 11106395]
[[Category: DNA-3-methyladenine glycosylase I]]
[[Category: DNA-3-methyladenine glycosylase I]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: protein-dna complex]]
[[Category: protein-dna complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:04:23 2008''

Revision as of 09:04, 20 March 2008


PDB ID 1f4r

Drag the structure with the mouse to rotate
, resolution 2.4Å
Ligands:
Activity: DNA-3-methyladenine glycosylase I, with EC number 3.2.2.20
Coordinates: save as pdb, mmCIF, xml



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


Contents

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. 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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