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1. 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