Conformational stability and activity of p73 require a second helix in the tetramerization domain.
|Abstract||p73 and p63, the two ancestral members of the p53 family, are involved in neurogenesis, epithelial stem cell maintenance and quality control of female germ cells. The highly conserved oligomerization domain (OD) of tumor suppressor p53 is essential for its biological functions, and its structure was believed to be the prototype for all three proteins. However, we report that the ODs of p73 and p63 differ from the OD of p53 by containing an additi ... [truncated at 450 characters in length]|
|Author||Coutandin, D; Löhr, F; Niesen, F H; et al|
|Subject||Amino Acid Sequence Animals Conserved Sequence DNA-Binding Proteins Humans Mice Models, Molecular Molecular Sequence Data Mutation Nuclear Magnetic Resonance, Biomolecular Nuclear Proteins Phosphoproteins Protein Multimerization Protein Structure, Quaternary Protein Structure, Secondary Sequence Alignment Thermodynamics Trans-Activators Tumor Suppressor Protein p53 Tumor Suppressor Proteins chemistry genetics metabolism chemistry genetics metabolism chemistry metabolism chemistry metabolism chemistry metabolism chemistry genetics metabolism|