Epitope analysis of the human p53 tumour suppressor protein
Language English Country Czech Republic Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
9158951
Knihovny.cz E-resources
- MeSH
- Epitopes analysis MeSH
- Humans MeSH
- Molecular Sequence Data MeSH
- Antibodies, Monoclonal MeSH
- Tumor Suppressor Protein p53 chemistry immunology MeSH
- Peptide Mapping MeSH
- Amino Acid Sequence MeSH
- Antibody Specificity MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Epitopes MeSH
- Antibodies, Monoclonal MeSH
- Tumor Suppressor Protein p53 MeSH
Using a set of overlapping peptides of the human p53 protein, we have performed an accurate mapping of the p53 antigenic sites, recognized by a panel of 19 monoclonal antibodies from the Bp53 series. The results show that most of the antibodies recognize determinants localized in the amino-terminal domain of the protein. Several antibodies reacted with peptides which correspond to the antigenic determinants localized in the carboxy terminus of p53. None of these antibodies reacted with peptides in the central DNA-binding domain of p53 protein.
Evidence for allosteric effects on p53 oligomerization induced by phosphorylation
