Ontology highlight
ABSTRACT:
SUBMITTER: Shan B
PROVIDER: S-EPMC3436289 | biostudies-literature | 2012 Aug
REPOSITORIES: biostudies-literature
Shan Bing B Li Da-Wei DW Brüschweiler-Li Lei L Brüschweiler Rafael R
The Journal of biological chemistry 20120717 36
The interaction between the transactivation domain of p53 (p53TAD) and the N-terminal domain of MDM2 and MDMX plays an essential role for cell function. Mutations in these proteins have been implicated in many forms of cancer. The intrinsically disordered p53TAD contains two subdomains, TAD1 and TAD2. Using NMR spectroscopy, site-directed mutagenesis, and molecular dynamics simulations, we demonstrate that TAD2 directly interacts with MDM2, adopting transient structures that bind to the same hyd ...[more]