Identification of Three Interactions to Determine the Conformation Change and to Maintain the Function of Kir2.1 Channel Protein
LI Jun-Wei1, XIAO Shao-Ying2, XIE Xiao-Xiao1, YU Hui1, ZHANG Hai-Lin3, ZHAN Yong1**, AN Hai-Long1**
1Key Laboratory of Molecular Biophysics of Hebei Province, Institute of Biophysics, School of Sciences, Hebei University of Technology, Tianjin 300401 2School of Architecture & Art Design, Hebei University of Technology, Tianjin 300401 3Key Laboratory of Neural and Vascular Biology (Ministry of Education), The Key Laboratory of Pharmacology and Toxicology for New Drug of Hebei Province, Department of Pharmacology, Hebei Medical University, Shijiazhuang 050017
Abstract：We find that a conserved mutation residue Glu to residue Asp (E303D), which both have the same polar and charged properties, makes Kir2.1 protein lose its function. To understand the mechanism, we identify three interactions which control the conformation change and maintain the function of the Kir2.1 protein by combining homology modeling and molecular dynamics with targeted molecular dynamics. We find that the E303D mutation weakens these interactions and results in the loss of the related function. Our data indicate that not only the amino residues but also the interactions determine the function of proteins.
. [J]. 中国物理快报, 2015, 32(02): 28702-028702.
LI Jun-Wei, XIAO Shao-Ying, XIE Xiao-Xiao, YU Hui, ZHANG Hai-Lin, ZHAN Yong, AN Hai-Long. Identification of Three Interactions to Determine the Conformation Change and to Maintain the Function of Kir2.1 Channel Protein. Chin. Phys. Lett., 2015, 32(02): 28702-028702.
2015, Vol. 32 
