Savva, Renos and McAuley-Hecht, K. and Brown, T. and Pearl, L. (1995) The structural basis of specific base-excision repair by uracil-DNA glycosylase. Nature 373 (6514), pp. 487-493. ISSN 0028-0836.
Abstract
The 1.75-Å 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.
Metadata
| Item Type: | Article |
|---|---|
| School: | Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences |
| Research Centres and Institutes: | Innovation Management Research, Birkbeck Centre for |
| Depositing User: | Sarah Hall |
| Date Deposited: | 14 May 2019 15:29 |
| Last Modified: | 02 Aug 2023 17:51 |
| URI: | https://eprints.bbk.ac.uk/id/eprint/27534 |
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