|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
6514
|
|
pubmed:dateCreated |
1995-3-3
|
|
pubmed:abstractText |
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.
|
|
pubmed:grant |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Feb
|
|
pubmed:issn |
0028-0836
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
9
|
|
pubmed:volume |
373
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
487-93
|
|
pubmed:dateRevised |
2009-9-29
|
|
pubmed:meshHeading |
pubmed-meshheading:7845459-Amino Acid Sequence,
pubmed-meshheading:7845459-Binding Sites,
pubmed-meshheading:7845459-Catalysis,
pubmed-meshheading:7845459-Computer Graphics,
pubmed-meshheading:7845459-Crystallography, X-Ray,
pubmed-meshheading:7845459-DNA Glycosylases,
pubmed-meshheading:7845459-DNA Repair,
pubmed-meshheading:7845459-Herpesvirus 1, Human,
pubmed-meshheading:7845459-Humans,
pubmed-meshheading:7845459-Models, Molecular,
pubmed-meshheading:7845459-Molecular Sequence Data,
pubmed-meshheading:7845459-N-Glycosyl Hydrolases,
pubmed-meshheading:7845459-Protein Structure, Secondary,
pubmed-meshheading:7845459-Structure-Activity Relationship,
pubmed-meshheading:7845459-Substrate Specificity,
pubmed-meshheading:7845459-Thymine,
pubmed-meshheading:7845459-Uracil,
pubmed-meshheading:7845459-Uracil-DNA Glycosidase
|
|
pubmed:year |
1995
|
|
pubmed:articleTitle |
The structural basis of specific base-excision repair by uracil-DNA glycosylase.
|
|
pubmed:affiliation |
Department of Biochemistry and Molecular Biology, University College London, UK.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
