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The 1.75-A crystal structure of the uracil-DNA glycosylase from herpes simplex virus type-1 reveals a new fold, distantly related to dinucleotide-binding proteins. Complexes with a trideoxynucleotide, and with uracil, define the DNA-binding site and allow a detailed understanding of the exquisitely specific recognition of uracil in DNA. The overall structure suggests binding models for elongated single- and double-stranded DNA substrates. Conserved residues close to the uracil-binding site suggest a catalytic mechanism for hydrolytic base excision.

Original publication




Journal article



Publication Date





487 - 493


Amino Acid Sequence, Binding Sites, Catalysis, Computer Graphics, Crystallography, X-Ray, DNA Glycosylases, DNA Repair, Herpesvirus 1, Human, Humans, Models, Molecular, Molecular Sequence Data, N-Glycosyl Hydrolases, Protein Structure, Secondary, Structure-Activity Relationship, Substrate Specificity, Thymine, Uracil, Uracil-DNA Glycosidase