Conformational changes of the p53-binding cleft of MDM2 revealed by molecular dynamics simulations.

Abstract

Two 35-ns molecular dynamics simulations of both ligated [mouse double minute protein 2 (MDM2(p53))] and unligated (MDM2(apo)) structures of human MDM2 bound to the N-terminal domain of the tumor suppressor p53 have been performed. Analysis of the dynamics revealed that the most flexible region of MDM2 was the p53-binding cleft. When MDM2 was bound to p53… (More)

Topics

Cite this paper

@article{EspinozaFonseca2006ConformationalCO, title={Conformational changes of the p53-binding cleft of MDM2 revealed by molecular dynamics simulations.}, author={L Michel Espinoza-Fonseca and Jos{\'e} Guadalupe Trujillo-Ferrara}, journal={Biopolymers}, year={2006}, volume={83 4}, pages={365-73} }