[HTML][HTML] Binding of p53 to the central domain of Mdm2 is regulated by phosphorylation
R Kulikov, M Winter, C Blattner - Journal of biological chemistry, 2006 - ASBMB
The Mdm2 protein is the major regulator of the tumor suppressor protein p53. We show that
the p53 protein associates both with the N-terminal and with the central domain of Mdm2.
The central p53-binding site of Mdm2 encompasses amino acids 235–300. Binding of p53 to
the central domain is significantly enhanced after phosphorylation of the central domain of
Mdm2. The N-terminal and central domains of Mdm2 act synergistically in binding to p53.
p53 mutants that have mutations in the tetramerization domain and that fail to oligomerize do …
the p53 protein associates both with the N-terminal and with the central domain of Mdm2.
The central p53-binding site of Mdm2 encompasses amino acids 235–300. Binding of p53 to
the central domain is significantly enhanced after phosphorylation of the central domain of
Mdm2. The N-terminal and central domains of Mdm2 act synergistically in binding to p53.
p53 mutants that have mutations in the tetramerization domain and that fail to oligomerize do …