Article
Two N-terminal self-association domains are required for the dominant negative transcriptional activity of WT1 Denys-Drash mutant proteins.
Biochemical and biophysical research communications - 28 Apr 1997
Holmes G, Boterashvili S, English M, Wainwright B, Licht J, Little M
Abstract excerpt
Patients with Denys-Drash syndrome (DDS) have been shown to be constitutionally heterozygous for mutations of the WT1 gene. Almost all DDS mutations inactivate or remove the DNA-binding zinc finger region of WT1 and the resulting mutant proteins appear to act in a dominant negative manner. This m...
Topics
- Base Sequence
- DNA-Binding Proteins
- Disorders of Sex Development
- Genes, Wilms Tumor
- Heterozygote
- Humans
- In Vitro Techniques
- Male
- Molecular Structure
- Mutation
- Oligodeoxyribonucleotides
- Protein Binding
- Recombinant Fusion Proteins
- Transcription Factors