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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 E303 D 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.
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. Know 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 E303 D 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.