The structural basis of specific base-excision repair by uracil-DNA glycosylase.

Article Details

Citation

Savva R, McAuley-Hecht K, Brown T, Pearl L

The structural basis of specific base-excision repair by uracil-DNA glycosylase.

Nature. 1995 Feb 9;373(6514):487-93.

PubMed ID
7845459 [ View in PubMed
]
Abstract

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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Uracil-DNA glycosylaseP10186Details