2oyt: Difference between revisions

Revision as of 06:03, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2oyt.png

Template:STRUCTURE 2oyt

Crystal Structure of UNG2/DNA(TM)Crystal Structure of UNG2/DNA(TM)

Template:ABSTRACT PUBMED 17704764

About this StructureAbout this Structure

2OYT is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Enzymatic capture of an extrahelical thymine in the search for uracil in DNA., Parker JB, Bianchet MA, Krosky DJ, Friedman JI, Amzel LM, Stivers JT, Nature. 2007 Sep 27;449(7161):433-7. Epub 2007 Aug 19. PMID:17704764

Page seeded by OCA on Mon Jul 28 06:03:15 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2oyt.gif|left|200px]]
+{{Seed}}
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 {{STRUCTURE_2oyt|  PDB=2oyt  |  SCENE=  }}
-'''Crystal Structure of UNG2/DNA(TM)'''
+===Crystal Structure of UNG2/DNA(TM)===
-==Overview==
+<!--
-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.
+-->
+{{ABSTRACT_PUBMED_17704764}}
 ==About this Structure==
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 [[Category: Hydrolase/dna complex]]
 [[Category: Ung2]]
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