1akz

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[[Image:1akz.gif|left|200px]]
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{{STRUCTURE_1akz| PDB=1akz | SCENE= }}
{{STRUCTURE_1akz| PDB=1akz | SCENE= }}
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'''HUMAN URACIL-DNA GLYCOSYLASE'''
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===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.
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(as it appears on PubMed at http://www.pubmed.gov), where 7697717 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7697717}}
==About this Structure==
==About this Structure==
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[[Category: Glycosylase]]
[[Category: Glycosylase]]
[[Category: Uracil removal from dna]]
[[Category: Uracil removal from dna]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:04:08 2008''

Revision as of 14:04, 30 June 2008

Template:STRUCTURE 1akz

HUMAN URACIL-DNA GLYCOSYLASE

Template:ABSTRACT PUBMED 7697717

About this Structure

1AKZ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis., Mol CD, Arvai AS, Slupphaug G, Kavli B, Alseth I, Krokan HE, Tainer JA, Cell. 1995 Mar 24;80(6):869-78. PMID:7697717

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