p53 is a powerful anti-tumoral molecule frequently inactivated by mutations ordeletions in cancer. However, half of all human tumors expresses wild-type p53, and itsactivation, by antagonizing its negative regulator Mdm2, might offer a new strategy fortherapeutic protocol. In this work, we present a molecular dynamics study on Mdm2 structurebound to two different known inhibitors with the aim to investigate the structural transitionsbetween apo-Mdm2 and Mdm2-inhibitor complexes. We tried to gain information aboutconformational changes binding a benzodiazepine derivative inhibitor with respect the knownnutlin and the apo form. The conformational changes alter the size of the cleft and were mainlyin the linker regions, suggesting that the overall dynamic nature of Mdm2 is related to dynamicmovements in these regions.
|Numero di pagine||7|
|Rivista||Biochemical and Biophysical Research Communications|
|Stato di pubblicazione||Published - 2012|
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology