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1. Simulation study on the molecular mechanism of RITA interaction with MDM2 and MDMX????? | |||
Qian Sinong,Jiang Quan,Hu Jing,Wu Qinghua | |||
Biology 08 April 2014 | |||
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Abstract:Inhibition of the interactions between the tumor suppressor protein p53 and its negative regulators, the MDM2 and MDMX oncogenic proteins, is increasingly gaining interest in cancer therapy and drug design. RITA a potential tumor suppressor molecular which can induce accumulation of P53 in tumor cells, but its mechanism is controversial and has rarely reports on MDMX interacting with RITA . In this study, we carried out molecular docking simulations on RITA to MDM2 and MDMX to find the possible mechanism of RITA. After molecular docking with DS3.0 programs, ten active sites have found in MDMX-RITA interaction, and one active site has found in MDM2-RITA interaction. Analysis of MDMX binding to RITA, active site 6 get higher scores. The CDOCKER_ENERGY is -33.27 kcal/mol; CDOCKER_INTERACTION_ENERGY is -41.10 kcal/mol; RMSD is 31.88 ?. And results of MDM2 binding to RITA are -20.15 kcal/mol , -28.09 kcal/mol and 33.93 ? in turn. There are three Hbonds between MDMX and RITA while only 1 between RTIA and MDM2.. The interacting amino-acid residues of MDMX are ASP79, LYS63, and LYS35.The amino-acid residue of MDM2 is LYS51.In conclusion, the intermolecular affinity between RITA and MDMX is better than MDM2, which means that RITA may bind to MDMX to activate p53 function in tumors. | |||
TO cite this article:Qian Sinong,Jiang Quan,Hu Jing, et al. Simulation study on the molecular mechanism of RITA interaction with MDM2 and MDMX?????[OL].[ 8 April 2014] http://en.paper.edu.cn/en_releasepaper/content/4592661 |
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