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1. A Fusion Protein of the p53 Transaction Domain and the p53-Binding Domain of the Oncoprotein MdmX as an Efficient System for High-Throughput Screening of MdmX Inhibitors

Author:
Qin, Lingyun,   et al.   ; Chen, Rong; Zhou, Jingjing; Chen, Yao; Huang, Yongqi; Liu, Huili; Su, Zhengding;     Show all 7 Authors
Source:
Biochemistry 2017 v.56 no.25 pp. 3273-3282
ISSN:
1520-4995
Subject:
amino acids; antineoplastic activity; drugs; fluorescence; fluorescence emission spectroscopy; ligands; models; neoplasms; oncogene proteins; screening; therapeutics
Abstract:
... In nearly half of cancers, the anticancer activity of p53 protein is often impaired by the overexpressed oncoprotein Mdm2 and its homologue, MdmX, demanding efficient therapeutics to disrupt the aberrant p53–MdmX/Mdm2 interactions to restore the p53 activity. While many potent Mdm2-specific inhibitors have already undergone clinical investigations, searching for MdmX-specific inhibitors has become ...
DOI:
10.1021/acs.biochem.7b00085

2. Effect of the Flexible Regions of the Oncoprotein Mouse Double Minute X on Inhibitor Binding Affinity

Author:
Qin, Lingyun,   et al.   ; Liu, Huili; Chen, Rong; Zhou, Jingjing; Cheng, Xiyao; Chen, Yao; Huang, Yongqi; Su, Zhengding;     Show all 8 Authors
Source:
Biochemistry 2017 v.56 no.44 pp. 5943-5954
ISSN:
1520-4995
Subject:
amino acid sequences; binding capacity; chemical interactions; drugs; engineering; ligands; mice; models; molecular dynamics; mutants; oncogene proteins; pharmacology; prediction; protein conformation; protein engineering; screening
Abstract:
... The oncoprotein MdmX (mouse double minute X) is highly homologous to Mdm2 (mouse double minute 2) in terms of their amino acid sequences and three-dimensional conformations, but Mdm2 inhibitors exhibit very weak affinity for MdmX, providing an excellent model for exploring how protein conformation distinguishes and alters inhibitor binding. The intrinsic conformation flexibility of proteins plays ...
DOI:
10.1021/acs.biochem.7b00903