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| [[Image:1akz.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1akz| PDB=1akz | SCENE= }} | | {{STRUCTURE_1akz| PDB=1akz | SCENE= }} |
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| '''HUMAN URACIL-DNA GLYCOSYLASE'''
| | ===HUMAN URACIL-DNA GLYCOSYLASE=== |
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| ==Overview==
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| Crystal structures of the DNA repair enzyme human uracil-DNA glycosylase (UDG), combined with mutational analysis, reveal the structural basis for the specificity of the enzyme. Within the classic alpha/beta fold of UDG, sequence-conserved residues form a positively charged, active-site groove the width of duplex DNA, at the C-terminal edge of the central four-stranded parallel beta sheet. In the UDG-6-aminouracil complex, uracil binds at the base of the groove within a rigid preformed pocket that confers selectivity for uracil over other bases by shape complementary and by main chain and Asn-204 side chain hydrogen bonds. Main chain nitrogen atoms are positioned to stabilize the oxyanion intermediate generated by His-268 acting via nucleophilic attack or general base mechanisms. Specific binding of uracil flipped out from a DNA duplex provides a structural mechanism for damaged base recognition.
| | The line below this paragraph, {{ABSTRACT_PUBMED_7697717}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 7697717 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_7697717}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Glycosylase]] | | [[Category: Glycosylase]] |
| [[Category: Uracil removal from dna]] | | [[Category: Uracil removal from dna]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:24:23 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:04:08 2008'' |