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| [[Image:2oyt.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2oyt| PDB=2oyt | SCENE= }} | | {{STRUCTURE_2oyt| PDB=2oyt | SCENE= }} |
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| '''Crystal Structure of UNG2/DNA(TM)'''
| | ===Crystal Structure of UNG2/DNA(TM)=== |
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| ==Overview==
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| The enzyme uracil DNA glycosylase (UNG) excises unwanted uracil bases in the genome using an extrahelical base recognition mechanism. Efficient removal of uracil is essential for prevention of C-to-T transition mutations arising from cytosine deamination, cytotoxic U*A pairs arising from incorporation of dUTP in DNA, and for increasing immunoglobulin gene diversity during the acquired immune response. A central event in all of these UNG-mediated processes is the singling out of rare U*A or U*G base pairs in a background of approximately 10(9) T*A or C*G base pairs in the human genome. Here we establish for the human and Escherichia coli enzymes that discrimination of thymine and uracil is initiated by thermally induced opening of T*A and U*A base pairs and not by active participation of the enzyme. Thus, base-pair dynamics has a critical role in the genome-wide search for uracil, and may be involved in initial damage recognition by other DNA repair glycosylases. | | The line below this paragraph, {{ABSTRACT_PUBMED_17704764}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17704764 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17704764}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Hydrolase/dna complex]] | | [[Category: Hydrolase/dna complex]] |
| [[Category: Ung2]] | | [[Category: Ung2]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:57:23 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:03:15 2008'' |