2oxm: Difference between revisions

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==Overview==
==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 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.
 
==Disease==
Known diseases associated with this structure: Immunodeficiency with hyper IgM, type 4 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191525 191525]]


==About this Structure==
==About this Structure==
2OXM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Known structural/functional Site: <scene name='pdbsite=AC1:4mf Binding Site For Residue C 27'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OXM OCA].  
2OXM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Known structural/functional Site: <scene name='pdbsite=AC1:4mf+Binding+Site+For+Residue+C+27'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OXM OCA].  


==Reference==
==Reference==
Line 13: Line 16:
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Amzel, L.M.]]
[[Category: Amzel, L M.]]
[[Category: Bianchet, M.A.]]
[[Category: Bianchet, M A.]]
[[Category: J.T., Stivers.]]
[[Category: J T., Stivers.]]
[[Category: Krosky, D.J.]]
[[Category: Krosky, D J.]]
[[Category: enzyme dna complex]]
[[Category: enzyme dna complex]]
[[Category: hydrolase/dna complex]]
[[Category: hydrolase/dna complex]]
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[[Category: uracil dna glycosylase]]
[[Category: uracil dna glycosylase]]


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